GenomeNet

Database: UniProt
Entry: PKNG_MYCTU
LinkDB: PKNG_MYCTU
Original site: PKNG_MYCTU 
ID   PKNG_MYCTU              Reviewed;         750 AA.
AC   P9WI73; L0T3M0; P65728; P96256;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Serine/threonine-protein kinase PknG;
DE            EC=2.7.11.1;
GN   Name=pknG; OrderedLocusNames=Rv0410c; ORFNames=MTCY22G10.06c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP   AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=15186418; DOI=10.1111/j.1365-2958.2004.04085.x;
RA   Cowley S., Ko M., Pick N., Chow R., Downing K.J., Gordhan B.G., Betts J.C.,
RA   Mizrahi V., Smith D.A., Stokes R.W., Av-Gay Y.;
RT   "The Mycobacterium tuberculosis protein serine/threonine kinase PknG is
RT   linked to cellular glutamate/glutamine levels and is important for growth
RT   in vivo.";
RL   Mol. Microbiol. 52:1691-1702(2004).
RN   [3]
RP   CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND
RP   MUTAGENESIS OF LYS-181.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=11496007; DOI=10.1099/00221287-147-8-2307;
RA   Koul A., Choidas A., Tyagi A.K., Drlica K., Singh Y., Ullrich A.;
RT   "Serine/threonine protein kinases PknF and PknG of Mycobacterium
RT   tuberculosis: characterization and localization.";
RL   Microbiology 147:2307-2314(2001).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH GARA,
RP   AND AUTOPHOSPHORYLATION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=19019160; DOI=10.1111/j.1365-2958.2008.06489.x;
RA   O'Hare H.M., Duran R., Cervenansky C., Bellinzoni M., Wehenkel A.M.,
RA   Pritsch O., Obal G., Baumgartner J., Vialaret J., Johnsson K., Alzari P.M.;
RT   "Regulation of glutamate metabolism by protein kinases in mycobacteria.";
RL   Mol. Microbiol. 70:1408-1423(2008).
RN   [5]
RP   FUNCTION IN ANTIBIOTIC RESISTANCE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=19528288; DOI=10.1128/aac.00012-09;
RA   Wolff K.A., Nguyen H.T., Cartabuke R.H., Singh A., Ogwang S., Nguyen L.;
RT   "Protein kinase G is required for intrinsic antibiotic resistance in
RT   mycobacteria.";
RL   Antimicrob. Agents Chemother. 53:3515-3519(2009).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, DOMAIN, PHOSPHORYLATION AT THR-63, AND MUTAGENESIS OF THR-63;
RP   CYS-106; CYS-109; CYS-128; CYS-131; LYS-181 AND THR-309.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=19638631; DOI=10.1074/jbc.m109.036095;
RA   Tiwari D., Singh R.K., Goswami K., Verma S.K., Prakash B., Nandicoori V.K.;
RT   "Key residues in Mycobacterium tuberculosis protein kinase G play a role in
RT   regulating kinase activity and survival in the host.";
RL   J. Biol. Chem. 284:27467-27479(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 74-750 IN COMPLEX WITH INHIBITOR
RP   AX20017, FUNCTION, ACTIVITY REGULATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP   ILE-87; ALA-92; CYS-106; CYS-109; CYS-128 AND CYS-131.
RX   PubMed=17616581; DOI=10.1073/pnas.0702842104;
RA   Scherr N., Honnappa S., Kunz G., Mueller P., Jayachandran R., Winkler F.,
RA   Pieters J., Steinmetz M.O.;
RT   "Structural basis for the specific inhibition of protein kinase G, a
RT   virulence factor of Mycobacterium tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12151-12156(2007).
CC   -!- FUNCTION: Phosphorylates GarA. May play a role in metabolic regulation
CC       via control of the phosphorylation status of GarA. Plays a crucial role
CC       in the survival of mycobacteria within host macrophages, by blocking
CC       the intracellular degradation of mycobacteria in lysosomes. Required
CC       for intrinsic antibiotic resistance. {ECO:0000269|PubMed:17616581,
CC       ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:19528288,
CC       ECO:0000269|PubMed:19638631}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000269|PubMed:11496007, ECO:0000269|PubMed:15186418,
CC         ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:19638631};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11496007,
CC         ECO:0000269|PubMed:15186418, ECO:0000269|PubMed:19019160,
CC         ECO:0000269|PubMed:19638631};
CC   -!- ACTIVITY REGULATION: Kinase activity is regulated by the redox status
CC       of the environment via the rubredoxin domain. Autophosphorylation is
CC       not essential for kinase activity, but it promotes binding to GarA. The
CC       C-terminal domain also contributes to the regulation of activity.
CC       Inhibited by a specific small molecular-weight inhibitor, the
CC       tetrahydrobenzothiophene AX20017. {ECO:0000269|PubMed:17616581,
CC       ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:19638631}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2122 nM for GarA {ECO:0000269|PubMed:19638631};
CC   -!- SUBUNIT: Homodimer. Interacts with the FHA domain of GarA.
CC       {ECO:0000269|PubMed:17616581, ECO:0000269|PubMed:19019160}.
CC   -!- INTERACTION:
CC       P9WI73; P9WJA9: garA; NbExp=6; IntAct=EBI-6405537, EBI-6405522;
CC       P9WI73; P9WI73: pknG; NbExp=4; IntAct=EBI-6405537, EBI-6405537;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Also detected in
CC       growth media, suggesting that it can be translocated into host
CC       macrophages under specific conditions.
CC   -!- DOMAIN: Contains an N-terminal rubredoxin domain, a central kinase
CC       domain and a C-terminal TPR domain. {ECO:0000269|PubMed:17616581,
CC       ECO:0000269|PubMed:19638631}.
CC   -!- PTM: Autophosphorylated. In vitro, incorporates up to four phosphate
CC       groups on Thr-23, Thr-32 and Thr-63 and/or Thr-64 and/or Ser-65. In
CC       vivo, is probably phosphorylated only on Thr-63.
CC       {ECO:0000269|PubMed:19638631}.
CC   -!- DISRUPTION PHENOTYPE: Disruption causes delayed mortality in mice.
CC       Mutant accumulates glutamate and glutamine.
CC       {ECO:0000269|PubMed:15186418}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; AL123456; CCP43141.1; -; Genomic_DNA.
DR   PIR; H70628; H70628.
DR   RefSeq; NP_214924.1; NC_000962.3.
DR   RefSeq; WP_003402100.1; NZ_NVQJ01000002.1.
DR   PDB; 2PZI; X-ray; 2.40 A; A/B=74-750.
DR   PDB; 4Y0X; X-ray; 1.74 A; A=74-405.
DR   PDB; 4Y12; X-ray; 1.90 A; A=74-405.
DR   PDB; 7Q52; X-ray; 2.35 A; AAA=74-405.
DR   PDBsum; 2PZI; -.
DR   PDBsum; 4Y0X; -.
DR   PDBsum; 4Y12; -.
DR   PDBsum; 7Q52; -.
DR   AlphaFoldDB; P9WI73; -.
DR   SMR; P9WI73; -.
DR   IntAct; P9WI73; 1.
DR   STRING; 83332.Rv0410c; -.
DR   BindingDB; P9WI73; -.
DR   ChEMBL; CHEMBL6070; -.
DR   DrugBank; DB07398; 2-[(CYCLOPROPYLCARBONYL)AMINO]-4,5,6,7-TETRAHYDRO-1-BENZOTHIOPHENE-3-CARBOXAMIDE.
DR   iPTMnet; P9WI73; -.
DR   PaxDb; 83332-Rv0410c; -.
DR   DNASU; 886397; -.
DR   GeneID; 886397; -.
DR   KEGG; mtu:Rv0410c; -.
DR   TubercuList; Rv0410c; -.
DR   eggNOG; COG0515; Bacteria.
DR   InParanoid; P9WI73; -.
DR   OMA; PHCGSAY; -.
DR   OrthoDB; 137117at2; -.
DR   PhylomeDB; P9WI73; -.
DR   BRENDA; 2.7.11.1; 3445.
DR   SABIO-RK; P9WI73; -.
DR   PRO; PR:P9WI73; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MTBBASE.
DR   GO; GO:0006538; P:glutamate catabolic process; IMP:MTBBASE.
DR   GO; GO:0006543; P:glutamine catabolic process; IMP:MTBBASE.
DR   GO; GO:0052064; P:induction by symbiont of defense-related host reactive oxygen species production; IMP:MTBBASE.
DR   GO; GO:0030682; P:mitigation of host defenses by symbiont; IMP:MTBBASE.
DR   GO; GO:0052027; P:perturbation of host signal transduction pathway; IMP:MTBBASE.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0052170; P:suppression of host innate immune response; IMP:MTBBASE.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   DisProt; DP01153; -.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR031634; PknG_rubred.
DR   InterPro; IPR031636; PknG_TPR.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24363:SF0; SERINE/THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF16919; PknG_rubred; 1.
DR   Pfam; PF16918; PknG_TPR; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; ATP-binding; Cell membrane; Cytoplasm;
KW   Direct protein sequencing; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   TPR repeat; Transferase; Virulence.
FT   CHAIN           1..750
FT                   /note="Serine/threonine-protein kinase PknG"
FT                   /id="PRO_0000171216"
FT   DOMAIN          151..396
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          536..569
FT                   /note="TPR"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        276
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         157..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         63
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:19638631"
FT   MUTAGEN         63
FT                   /note="T->A: Lack of phosphorylation. Does not affect
FT                   kinase activity."
FT                   /evidence="ECO:0000269|PubMed:19638631"
FT   MUTAGEN         87
FT                   /note="I->S: Decreases inhibition by AX20017; when
FT                   associated with S-92."
FT                   /evidence="ECO:0000269|PubMed:17616581"
FT   MUTAGEN         92
FT                   /note="A->S: Decreases inhibition by AX20017; when
FT                   associated with S-87."
FT                   /evidence="ECO:0000269|PubMed:17616581"
FT   MUTAGEN         106
FT                   /note="C->A: Decrease in activity; when associated with A-
FT                   109; A-128 and A-131."
FT                   /evidence="ECO:0000269|PubMed:17616581,
FT                   ECO:0000269|PubMed:19638631"
FT   MUTAGEN         106
FT                   /note="C->S: Lack of activity; when associated with S-109;
FT                   S-128 and S-131."
FT                   /evidence="ECO:0000269|PubMed:17616581,
FT                   ECO:0000269|PubMed:19638631"
FT   MUTAGEN         109
FT                   /note="C->A: Decrease in activity; when associated with A-
FT                   106; A-128 and A-131."
FT                   /evidence="ECO:0000269|PubMed:17616581,
FT                   ECO:0000269|PubMed:19638631"
FT   MUTAGEN         109
FT                   /note="C->S: Lack of activity; when associated with S-106;
FT                   S-128 and S-131."
FT                   /evidence="ECO:0000269|PubMed:17616581,
FT                   ECO:0000269|PubMed:19638631"
FT   MUTAGEN         128
FT                   /note="C->A: Decrease in activity; when associated with A-
FT                   106; A-109 and A-131."
FT                   /evidence="ECO:0000269|PubMed:17616581,
FT                   ECO:0000269|PubMed:19638631"
FT   MUTAGEN         128
FT                   /note="C->S: Lack of activity; when associated with S-106;
FT                   S-109 and S-131."
FT                   /evidence="ECO:0000269|PubMed:17616581,
FT                   ECO:0000269|PubMed:19638631"
FT   MUTAGEN         131
FT                   /note="C->A: Decrease in activity; when associated with A-
FT                   106; A-109 and A-128."
FT                   /evidence="ECO:0000269|PubMed:17616581,
FT                   ECO:0000269|PubMed:19638631"
FT   MUTAGEN         131
FT                   /note="C->S: Lack of activity; when associated with S-106;
FT                   S-109 and S-128."
FT                   /evidence="ECO:0000269|PubMed:17616581,
FT                   ECO:0000269|PubMed:19638631"
FT   MUTAGEN         181
FT                   /note="K->M: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:11496007,
FT                   ECO:0000269|PubMed:19638631"
FT   MUTAGEN         309
FT                   /note="T->A,D,E: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:19638631"
FT   MUTAGEN         309
FT                   /note="T->S: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:19638631"
FT   TURN            75..78
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   STRAND          79..82
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   TURN            107..109
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          124..127
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   TURN            129..131
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   TURN            148..150
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          151..160
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          163..170
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   TURN            171..175
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          177..183
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           189..199
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           200..204
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          213..220
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          226..233
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           250..269
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           279..281
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          289..291
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           294..296
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   TURN            310..312
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           317..320
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           324..339
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           358..362
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           364..373
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           378..380
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   HELIX           385..403
FT                   /evidence="ECO:0007829|PDB:4Y0X"
FT   STRAND          413..415
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   STRAND          423..425
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           426..429
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           430..432
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           433..436
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           446..452
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           465..470
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   TURN            471..473
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           476..487
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           503..515
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           518..532
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           536..549
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           552..565
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           571..583
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           591..598
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           603..615
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           619..627
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           636..646
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           658..669
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           678..693
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   STRAND          699..703
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   STRAND          706..709
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           710..727
FT                   /evidence="ECO:0007829|PDB:2PZI"
FT   HELIX           731..744
FT                   /evidence="ECO:0007829|PDB:2PZI"
SQ   SEQUENCE   750 AA;  81577 MW;  CFC6E54DBE19569F CRC64;
     MAKASETERS GPGTQPADAQ TATSATVRPL STQAVFRPDF GDEDNFPHPT LGPDTEPQDR
     MATTSRVRPP VRRLGGGLVE IPRAPDIDPL EALMTNPVVP ESKRFCWNCG RPVGRSDSET
     KGASEGWCPY CGSPYSFLPQ LNPGDIVAGQ YEVKGCIAHG GLGWIYLALD RNVNGRPVVL
     KGLVHSGDAE AQAMAMAERQ FLAEVVHPSI VQIFNFVEHT DRHGDPVGYI VMEYVGGQSL
     KRSKGQKLPV AEAIAYLLEI LPALSYLHSI GLVYNDLKPE NIMLTEEQLK LIDLGAVSRI
     NSFGYLYGTP GFQAPEIVRT GPTVATDIYT VGRTLAALTL DLPTRNGRYV DGLPEDDPVL
     KTYDSYGRLL RRAIDPDPRQ RFTTAEEMSA QLTGVLREVV AQDTGVPRPG LSTIFSPSRS
     TFGVDLLVAH TDVYLDGQVH AEKLTANEIV TALSVPLVDP TDVAASVLQA TVLSQPVQTL
     DSLRAARHGA LDADGVDFSE SVELPLMEVR ALLDLGDVAK ATRKLDDLAE RVGWRWRLVW
     YRAVAELLTG DYDSATKHFT EVLDTFPGEL APKLALAATA ELAGNTDEHK FYQTVWSTND
     GVISAAFGLA RARSAEGDRV GAVRTLDEVP PTSRHFTTAR LTSAVTLLSG RSTSEVTEEQ
     IRDAARRVEA LPPTEPRVLQ IRALVLGGAL DWLKDNKAST NHILGFPFTS HGLRLGVEAS
     LRSLARVAPT QRHRYTLVDM ANKVRPTSTF
//
DBGET integrated database retrieval system