GenomeNet

Database: UniProt
Entry: P40806
LinkDB: P40806
Original site: P40806 
ID   PKSJ_BACSU              Reviewed;        5043 AA.
AC   P40806; P40803;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 3.
DT   24-JAN-2024, entry version 163.
DE   RecName: Full=Polyketide synthase PksJ;
DE            Short=PKS;
GN   Name=pksJ; Synonyms=pksK; OrderedLocusNames=BSU17180;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / PB1424;
RX   PubMed=7704258; DOI=10.1099/13500872-141-2-299;
RA   Albertini A.M., Caramori T., Scoffone F., Scotti C., Galizzi A.;
RT   "Sequence around the 159 degree region of the Bacillus subtilis genome: the
RT   pksX locus spans 33.6 kb.";
RL   Microbiology 141:299-309(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT   the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
RN   [4]
RP   SEQUENCE REVISION TO 87; 619 AND 4981.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   FUNCTION AS AN ACYL CARRIER PROTEIN, AND PHOSPHOPANTETHEINYLATION AT
RP   SER-1689.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=16460000; DOI=10.1021/bi052333k;
RA   Dorrestein P.C., Blackhall J., Straight P.D., Fischbach M.A.,
RA   Garneau-Tsodikova S., Edwards D.J., McLaughlin S., Lin M., Gerwick W.H.,
RA   Kolter R., Walsh C.T., Kelleher N.L.;
RT   "Activity screening of carrier domains within nonribosomal peptide
RT   synthetases using complex substrate mixtures and large molecule mass
RT   spectrometry.";
RL   Biochemistry 45:1537-1546(2006).
RN   [6]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=17190806; DOI=10.1073/pnas.0609073103;
RA   Straight P.D., Fischbach M.A., Walsh C.T., Rudner D.Z., Kolter R.;
RT   "A singular enzymatic megacomplex from Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:305-310(2007).
RN   [7]
RP   FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=17234808; DOI=10.1073/pnas.0610503104;
RA   Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R.,
RA   Walsh C.T., Clardy J.;
RT   "The identification of bacillaene, the product of the PksX megacomplex in
RT   Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007).
CC   -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC       antibiotic polyketide bacillaene which is involved in secondary
CC       metabolism. {ECO:0000269|PubMed:16460000, ECO:0000269|PubMed:17234808}.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000305};
CC       Note=Binds 5 phosphopantetheines covalently. {ECO:0000305};
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
CC   -!- MISCELLANEOUS: The acyl carrier 2 domain binds glycine.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be two separate ORFs named pksJ and
CC       pksK. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U11039; AAA85143.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U11039; AAA85144.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL009126; CAB13589.3; -; Genomic_DNA.
DR   PIR; A69679; A69679.
DR   PIR; H69678; H69678.
DR   RefSeq; NP_389598.3; NC_000964.3.
DR   RefSeq; WP_003245563.1; NZ_JNCM01000035.1.
DR   PDB; 4J1Q; X-ray; 2.35 A; A=2669-3111.
DR   PDB; 4J1S; X-ray; 3.01 A; A=2669-3111.
DR   PDB; 4NA1; X-ray; 1.95 A; A/B=3336-3951.
DR   PDB; 4NA2; X-ray; 2.30 A; A/B=3336-3951.
DR   PDB; 4NA3; X-ray; 2.89 A; A/B=3336-3951.
DR   PDB; 5KTK; X-ray; 1.98 A; A=3954-4472.
DR   PDBsum; 4J1Q; -.
DR   PDBsum; 4J1S; -.
DR   PDBsum; 4NA1; -.
DR   PDBsum; 4NA2; -.
DR   PDBsum; 4NA3; -.
DR   PDBsum; 5KTK; -.
DR   SMR; P40806; -.
DR   DIP; DIP-60662N; -.
DR   IntAct; P40806; 7.
DR   STRING; 224308.BSU17180; -.
DR   PaxDb; 224308-BSU17180; -.
DR   EnsemblBacteria; CAB13589; CAB13589; BSU_17180.
DR   GeneID; 940043; -.
DR   KEGG; bsu:BSU17180; -.
DR   PATRIC; fig|224308.179.peg.1863; -.
DR   eggNOG; COG0300; Bacteria.
DR   eggNOG; COG0318; Bacteria.
DR   eggNOG; COG1020; Bacteria.
DR   eggNOG; COG1028; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   InParanoid; P40806; -.
DR   OMA; LFFEHET; -.
DR   OrthoDB; 2897140at2; -.
DR   PhylomeDB; P40806; -.
DR   BioCyc; BSUB:BSU17180-MONOMER; -.
DR   UniPathway; UPA01003; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd12116; A_NRPS_Ta1_like; 1.
DR   CDD; cd05906; A_NRPS_TubE_like; 1.
DR   CDD; cd20484; C_PKS-NRPS_PksJ-like; 1.
DR   CDD; cd08953; KR_2_SDR_x; 2.
DR   CDD; cd00833; PKS; 3.
DR   Gene3D; 1.10.1240.100; -; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 3.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 5.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 2.
DR   Pfam; PF00109; ketoacyl-synt; 3.
DR   Pfam; PF02801; Ketoacyl-synt_C; 3.
DR   Pfam; PF08659; KR; 2.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 5.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 2.
DR   SMART; SM00825; PKS_KS; 3.
DR   SMART; SM00823; PKS_PP; 5.
DR   SMART; SM01294; PKS_PP_betabranch; 4.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 5.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR   SUPFAM; SSF53901; Thiolase-like; 3.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 5.
DR   PROSITE; PS00606; KS3_1; 2.
DR   PROSITE; PS52004; KS3_2; 3.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
DR   PROSITE; PS52019; PKS_MFAS_DH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Antibiotic biosynthesis; Coiled coil;
KW   Cytoplasm; Ligase; Multifunctional enzyme; NADP; Phosphopantetheine;
KW   Phosphoprotein; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..5043
FT                   /note="Polyketide synthase PksJ"
FT                   /id="PRO_0000193184"
FT   DOMAIN          590..667
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1654..1729
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1760..2186
FT                   /note="Ketosynthase family 3 (KS3) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   DOMAIN          2374..2661
FT                   /note="PKS/mFAS DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   DOMAIN          3114..3188
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3212..3286
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3339..3779
FT                   /note="Ketosynthase family 3 (KS3) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   DOMAIN          4459..4536
FT                   /note="Carrier 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          4588..4992
FT                   /note="Ketosynthase family 3 (KS3) 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   REGION          141..481
FT                   /note="Adenylation 1"
FT   REGION          690..989
FT                   /note="Condensation"
FT                   /evidence="ECO:0000250"
FT   REGION          1181..1578
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2374..2499
FT                   /note="N-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          2513..2661
FT                   /note="C-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          3291..3314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          3839..3872
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        1932
FT                   /note="For beta-ketoacyl synthase 1 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        2068
FT                   /note="For beta-ketoacyl synthase 1 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        2108
FT                   /note="For beta-ketoacyl synthase 1 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        2403
FT                   /note="Proton acceptor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        2575
FT                   /note="Proton donor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        3511
FT                   /note="For beta-ketoacyl synthase 2 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        3646
FT                   /note="For beta-ketoacyl synthase 2 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        3695
FT                   /note="For beta-ketoacyl synthase 2 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        4743
FT                   /note="For beta-ketoacyl synthase 3 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         627
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1689
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000269|PubMed:16460000"
FT   MOD_RES         3148
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3246
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4496
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   CONFLICT        87
FT                   /note="V -> W (in Ref. 1; AAA85143)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        619
FT                   /note="N -> NAN (in Ref. 1; AAA85144)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4981
FT                   /note="D -> G (in Ref. 1; AAA85144)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2669..2678
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2692..2700
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2703..2712
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   TURN            2713..2715
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2716..2721
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2728..2745
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2747..2752
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2755..2762
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2767..2772
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2773..2783
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2787..2796
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   TURN            2797..2799
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2803..2811
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2818..2822
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2825..2833
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2848..2855
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   TURN            2856..2858
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2860..2873
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2877..2881
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2888..2899
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2903..2906
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2914..2927
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2933..2936
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   TURN            2946..2948
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2951..2958
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   TURN            2959..2962
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2963..2971
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   TURN            2972..2974
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          2978..2985
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2986..2990
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           2996..3017
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          3023..3030
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           3044..3052
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           3059..3072
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          3075..3082
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   HELIX           3084..3091
FT                   /evidence="ECO:0007829|PDB:4J1Q"
FT   STRAND          3342..3351
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3354..3356
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3357..3365
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   TURN            3376..3378
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3381..3384
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   TURN            3388..3390
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3399..3401
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3406..3409
FT                   /evidence="ECO:0007829|PDB:4NA2"
FT   HELIX           3411..3414
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3418..3421
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3426..3442
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3446..3449
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3455..3459
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3465..3471
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3480..3484
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3489..3498
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3504..3507
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3510..3512
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3513..3526
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3531..3539
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3545..3552
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3577..3585
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3586..3592
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3597..3607
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3619..3633
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3637..3639
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3642..3644
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3653..3669
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3679..3681
FT                   /evidence="ECO:0007829|PDB:4NA2"
FT   STRAND          3684..3687
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3690..3693
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3697..3699
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3700..3713
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3724..3726
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3735..3739
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3752..3754
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3760..3766
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3770..3778
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3795..3803
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3804..3819
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3825..3827
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3828..3837
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3843..3852
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3853..3865
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3870..3877
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3878..3880
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3884..3890
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3892..3903
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3907..3915
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   HELIX           3922..3925
FT                   /evidence="ECO:0007829|PDB:4NA1"
FT   STRAND          3969..3979
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          3990..3996
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           3998..4000
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4001..4008
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4012..4018
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4031..4033
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4034..4039
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4041..4043
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4053..4063
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4069..4077
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4091..4103
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4107..4114
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4120..4131
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4138..4143
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4146..4154
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   TURN            4156..4158
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4172..4177
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4182..4194
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4199..4205
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4211..4217
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4223..4236
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4240..4245
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4251..4264
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4268..4273
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4285..4287
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4290..4297
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   TURN            4298..4301
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4302..4311
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4319..4324
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4325..4327
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4330..4333
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4337..4353
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   TURN            4354..4356
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4359..4364
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4367..4370
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4378..4383
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4390..4402
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   STRAND          4407..4414
FT                   /evidence="ECO:0007829|PDB:5KTK"
FT   HELIX           4421..4423
FT                   /evidence="ECO:0007829|PDB:5KTK"
SQ   SEQUENCE   5043 AA;  562814 MW;  F6E8A8533D518DE4 CRC64;
     MRNNDNIRIL TNPSVSHGEP LHISEKQPAT IPEVLYRTAT ELGDTKGIIY LQPDGTEVYQ
     SYRRLWDDGL RIAKGLRQSG LKAKQSVILQ LGDNSQLLPA FWGCVLTGVV PAPLAVPPTY
     AESSSGTQKL KDAWTLLDKP AVITDRGMHQ EMLDWAKEQG LEGFRAIIVE DLLSAEADTD
     WHQSSPEDLA LLLLTSGSTG TPKAVMLNHR NIMSMVKGII QMQGFTREDI TFNWMPFDHV
     GGIGMLHLRD VYLGCQEINV SSETILMEPL KWLDWIDHYR ASVTWAPNFA FGLVTDFAEE
     IKDKKWDLSS MRYMLNGGEA MVAKVGRRIL ELLEPHGLPA DAIRPAWGMS ETSSGVIFSH
     EFTRAGTSDD DHFVEIGSPI PGFSMRIVND HNELVEEGEI GRFQVSGLSV TSGYYQRPDL
     NESVFTEDGW FETGDLGFLR NGRLTITGRT KDAIIINGIN YYSHAIESAV EELPEIETSY
     TAACAVRLGQ NSTDQLAIFF VTSAKLNDEQ MSQLLRNIQS HVSQVIGVTP EYLLPVQKEE
     IPKTAIGKIQ RTQLKTSFEN GEFDHLLHKP NRMNDAVQDE GIQQADQVKR VREEIQKHLL
     TCLTEELHVS HDWVEPNANI QSLGVNSIKM MKLIRSIEKN YHIKLTAREI HQYPTIERLA
     SYLSEHEDLS SLSADKKGTD TYKTEPERSQ ATFQPLSEVQ KGLWTLQKMS PEKSAYHVPL
     CFKFSSGLHH ETFQQAFGLV LNQHPILKHV IQEKDGVPFL KNEPALSIEI KTENISSLKE
     SDIPAFLRKK VKEPYVKENS PLVRVMSFSR SEQEHFLLVV IHHLIFDGVS SVTFIRSLFD
     TYQLLLKGQQ PEKAVSPAIY HDFAAWEKNM LAGKDGVKHR TYWQKQLSGT LPNLQLPNVS
     ASSVDSQFRE DTYTRRLSSG FMNQVRTFAK EHSVNVTTVF LSCYMMLLGR YTGQKEQIVG
     MPAMVRPEER FDDAIGHFLN MLPIRSELNP ADTFSSFISK LQLTILDGLD HAAYPFPKMV
     RDLNIPRSQA GSPVFQTAFF YQNFLQSGSY QSLLSRYADF FSVDFVEYIH QEGEYELVFE
     LWETEEKMEL NIKYNTGLFD AASISAMFDH FVYVTEQAML NPSQPLKEYS LLPEAEKQMI
     LKTWNATGKT YPYITFHELF EQQAKKTPDR AAVSYEGQTL TYRELDEKST QLAIYLQAHG
     VGPDRLAGIY VDRSLDMLVG LLAILKAGGA YVPLDPSYPA ERLEYMLEDS EVFITLTTSE
     LVNTLSWNGV TTALLDQDWD EIAQTASDRK VLTRTVTPEN LAYVIYTSGS TGKPKGVMIP
     HKALTNFLVS MGETPGLTAE DKMLAVTTYC FDIAALELFL PLIKGAHCYI CQTEHTKDVE
     KLKRDIRAIK PTVMQATPAT WKMLFYSGWE NEESVKILCG GEALPETLKR YFLDTGSEAW
     NMFGPTETTI WSAVQRINVE CSHATIGRPI ANTQIYITDS QLAPVPAGVP GELCIAGDGV
     AKGYYKKEEL TDSRFIDNPF EPGSKLYRTG DMARWLTGGR IEYIGRIDNQ VKIRGFRIEL
     GDIESRLSEH PGILECVVVA DMDNLAAYYT AKHANASLTA RELRHFVKNA LPAYMVPSYF
     IQLDHMPLTP NGKIDRNSLK NIDLSGEQLK QRQTSPKNIQ DTVFTIWQEV LKTSDIEWDD
     GFFDVGGDSL LAVTVADRIK HELSCEFSVT DLFEYSTIKN ISQYITEQRM GDASDHIPTD
     PAAHIEDQST EMSDLPDYYD DSVAIIGISC EFPGAKNHDE FWENLRDGKE SIAFFNKEEL
     QRFGISKEIA ENADYVPAKA SIDGKDRFDP SFFQISPKDA EFMDPQLRML LTHSWKAIED
     AGYAARQIPQ TSVFMSASNN SYRALLPSDT TESLETPDGY VSWVLAQSGT IPTMISHKLG
     LRGPSYFVHA NCSSSLIGLH SAYKSLLSGE SDYALVGGAT LHTESNIGYV HQPGLNFSSD
     GHIKAFDASA DGMIGGEGVA VVLLKKAADA VKDGDHIYAL LRGIGVNNDG ADKVGFYAPS
     VKGQADVVQQ VMNQTKVQPE SICYVEAHGT GTKLGDPIEL AALTNVYRQY TNKTQFCGIG
     SVKTNIGHLD TAAGLAGCIK VVMSLYHQEL APSVNYKEPN PNTDLASSPF YVVDQKKTLS
     REIKTHRAAL SSFGLGGTNT HAIFEQFKRD SDKGKIDGTC IVPISAKNKE RLQEYAEDIL
     AYLERRGFEN SQLPDFAYTL QVGREAMEHR VVFIADHVNE LKQRLTDFIN GNTAIEGCFQ
     GSKHNAREVS WLTEDEDSAE LIRKWMAKGK VNKLAEMWSK GAHIDWMQLY KGERPNRMSL
     PTYPFAKERY WPSQDDRKPV AQISGNQTGI GSIHPLLHQN TSDFSEQKFS SVFTGDEFFL
     RDHVVRGKPV LPGVAYLEMA YAAINQAAGS EIGQDVRIRL NHTVWVQPVV VDRHSAQVDI
     SLFPEEDGKI TFDIYSTQED GDDPVIHSQG SAELASAAET PVADLTEMSR RCGKGKMSPD
     QFYEEGRSRG MFHGPAFQGI KNVNIGNREV LAQLQLPEIV SGTNEQFVLH PSIMDSALQT
     ATICIMQELT DQKLILPFAL EELEVIKGCS SSMWAYARLS DSDHSGGVVQ KADIDVIDES
     GTVCVRIKGF STRVLEGEVH TSKPSTRHER LMLEPVWEKQ NEEREDEDLS YTEHIIVLFE
     TERSVTDSIA SHMKDARVIT LNEAVGHIAE RYQCYMQNIF ELLQSKVRKL SAGRIIIQAI
     VPLEKEKQLF AGVSGLFKTA EIEFSKLTAQ VIEIEKPEEM IDLHLKLKDD SRRPFDKQIR
     YEAGYRFVKG WREMVLPSAD TLHMPWRDEG VYLITGGAGS LGLLFAKEIA NRTGRSTIVL
     TGRSVLSEDK ENELEALRSI GAEVVYREAD VSDQHAVRHL LEEIKERYGT LNGIIHGAGS
     SKDRFIIHKT NEEFQEVLQP KVSGLLHVDE CSKDFPLDFF IFFSSVSGCL GNAGQADYAA
     ANSFMDAFAE YRRSLAASKK RFGSTISFNW PLWEEGGMQV GAEDEKRMLK TTGMVPMPTD
     SGLKAFYQGI VSDKPQVFVM EGQLQKMKQK LLSAGSKAKR NDQRKADQDQ GQTRKLEAAL
     IQMVGAILKV NTDDIDVNTE LSEYGFDSVT FTVFTNKINE KFQLELTPTI FFEYGSVQSL
     AEYVVAAYQG EWNQDATAKG KDERTNLVHS LSSLEASLSN MVSAILKVNS EDIDVNTELS
     EYGFDSVTFT VFTNKINEEF QLELTPTIFF EYGSLHSLAE YLTVEHGDTL VQEREKPEGQ
     EELQTKSSEA PKITSRRKRR FTQPIIAKAE RNKKQAADFE PVAIVGISGR FPGAMDIDEF
     WKNLEEGKDS ITEVPKDRWD WREHYGNPDT DVNKTDIKWG GFIDGVAEFD PLFFGISPRE
     ADYVDPQQRL LMTYVWKALE DAGCSPQSLS GTGTGIFIGT GNTGYKDLFH RANLPIEGHA
     ATGHMIPSVG PNRMSYFLNI HGPSEPVETA CSSSLVAIHR AVTAMQNGDC EMAIAGGVNT
     ILTEEAHISY SKAGMLSTDG RCKTFSADAN GYVRGEGVGM VMLKKLEDAE RDGNHIYGVI
     RGTAENHGGR ANTLTSPNPK AQADLLVRAY RQADIDPSTV TYIEAHGTGT ELGDPIEING
     LKAAFKELSN MRGESQPDVP DHRCGIGSVK SNIGHLELAA GISGLIKVLL QMKHKTLVKS
     LHCETLNPYL QLTDSPFYIV QEKQEWKSVT DRDGNELPRR AGISSFGIGG VNAHIVIEEY
     MPKANSEHTA TEQPNVIVLS AKNKSRLIDR ASQLLEVIRN KKYTDQDLHR IAYTLQVGRE
     EMDERLACVA GTMQELEEKL QAFVDGKEET DEFFRGQSHR NKETQTIFTA DEDMALALDA
     WIRKRKYAKL ADLWVKGVSI QWNTLYGETK PRLISLPSYP FAKDHYWVPA KEHSERDKKE
     LVNAIEDRAA CFLTKQWSLS PIGSAVPGTR TVAILCCQET ADLAAEVSSY FPNHLLIDVS
     RIENDQSDID WKEFDGLVDV IGCGWDDEGR LDWIEWVQRL VEFGHKEGLR LLCVTKGLES
     FQNTSVRMAG ASRAGLYRML QCEYSHLISR HMDAEEVTDH RRLAKLIADE FYSDSYDAEV
     CYRDGLRYQA FLKAHPETGK ATEQSAVFPK DHVLLITGGT RGIGLLCARH FAECYGVKKL
     VLTGREQLPP REEWARFKTS NTSLAEKIQA VRELEAKGVQ VEMLSLTLSD DAQVEQTLQH
     IKRTLGPIGG VIHCAGLTDM DTLAFIRKTS DDIQRVLEPK VSGLTTLYRH VCNEPLQFFV
     LFSSVSAIIP ELSAGQADYA MANSYMDYFA EAHQKHAPII SVQWPNWKET GMGEVTNQAY
     RDSGLLSITN SEGLRFLDQI VSKKFGPVVL PAMANQTNWE PELLMKRRKP HEGGLQEAAL
     QSPPARDIEE ADEVSKCDGL LSETQSWLID LFTEELRIDR EDFEIDGLFQ DYGVDSIILA
     QVLQRINRKL EAALDPSILY EYPTIQRFAD WLIGSYSERL SALFGGRISD ASAPLENKIE
     AEASVPGKDR ALTPQIQAPA ILSPDSHAEG IAVVGLSCRF PGAETLESYW SLLSEGRSSI
     GPIPAERWGC KTPYYAGVID GVSYFDPDFF LLHEEDVRAM DPQALLVLEE CLKLLYHAGY
     TPEEIKGKPV GVYIGGRSQH KPDEDSLDHA KNPIVTVGQN YLAANLSQFF DVRGPSVVVD
     TACSSALVGM NMAIQALRGG DIQSAIVGGV SLLSSDASHR LFDRRGILSK HSSFHVFDER
     ADGVVLGEGV GMVMLKTVKQ ALEDGDIIYA VVKAASVNND GRTAGPATPN LEAQKEVMKD
     ALFKSGKKPE DISYLEANGS GSIVTDLLEL KAIQSVYRSG HSSPLSLGSI KPNIGHPLCA
     EGIASFIKVV LMLKERRFVP FLSGEKEMAH FDQQKANITF SRALEKWTDS QPTAAINCFA
     DGGTNAHVIV EAWEKDEKHA IKRSPISPPQ LKKRMLSPGE PKLEAETSKM TAANIWDTYE
     VEV
//
DBGET integrated database retrieval system