ID C7Q4Y7_CATAD Unreviewed; 1769 AA.
AC C7Q4Y7;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:ACU73935.1};
GN OrderedLocusNames=Caci_5075 {ECO:0000313|EMBL:ACU73935.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU73935.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU73935.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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; CP001700; ACU73935.1; -; Genomic_DNA.
DR STRING; 479433.Caci_5075; -.
DR KEGG; cai:Caci_5075; -.
DR eggNOG; COG0477; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_49_0_11; -.
DR InParanoid; C7Q4Y7; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd17646; A_NRPS_AB3403-like; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR CDD; cd06173; MFS_MefA_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1366..1387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1399..1419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1425..1446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1458..1481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1487..1511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1544..1567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1579..1600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1607..1624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1630..1653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1665..1684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1696..1715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 954..1029
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 934..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1769 AA; 191904 MW; 8B93572054AF5492 CRC64;
MPPLSFAQER LWFMEQLAPG SAAHTVPVAL RLRGALDPDA FGRALRDLAG RHETLRMSYP
ADTDDRPGIH VAAAGEVPLR ISDADSLDAA QDVVGAMIAE PFDIVRGPVA RALLVRLADD
DHVLALAVHH IACDGWSVDV LLTDLFALYE ARLAGAPSTL PEPAIGYGDY AIWQRDRPGY
DTDHAYWAAQ LAGLPTLDLV TDRIRPPEQT YNGAAHGFRL NRTLTDSVKA LADRSQATPY
MVLLAAFQAL LARYTSQDDF AVGSPVAGRT LPELEPLVGC FVNMLTMRAD LTGRPSFTDL
LARVQETASA AYDHQELPFE QLVQRLDLPR DVARAPLFQV IFAMQNYQRG SAAGASGTLS
AEPFPLTSWA TRYDLELYIS QDGDALDALF VYNTDLFGAE TIARLANHFT ALLTAALDAP
ELPVADAEML DAAERARLLA DFNATTSDFP QDKTLHELVE AQCARTPDAV AIEFEGESLT
YREVNTQADA VAYRLSELGV GPESLVAVCA ERSLALPVAL LGVLKSGAAY LPLDPEYPPD
RLAFMLADAG VPVILAQRGL LDQLPETSAT IQYLDEATNL AAPPGWRAPR GDLAYAIYTS
GSTGRPKGVL NTHRAIVNRL DWMQRRYQLT ADDVVLQKTP AGFDVSVWEF FWPLLAGARL
VLARPGGHKD AGYLRDLIRS AGVTTAHFVP SMLGVFLAEE GVEQCRGLRR ILCSGEELPV
DVALRCLATL PAELHNLYGP TEAAIDVSSW QCTPQELTAA ARVPIGLPIQ NLALHVLDPQ
MQPVPIGVPG ELFLGGVGLA RGYLKRPALT AERFVPDPFG TPGSRLYRTG DLARRRTDGA
VEFLGRIDGQ VKIRGLRIEL GEIEAALRDQ PGVADAAAVV REDVPGDRRI VGYVVGEADH
AALRTALKQR LPDYMVPSAL VTLDVLPLTP NGKLDRRALP EPQRGRDEGT AFAAPESDSQ
RLIAQIWSDV LRVERIGIDD DFFDLGGHSL LAAQVVAKLR RSAGAGVSVL DLFKNPTVRG
LATLLDTPAA ERGPAELVHE LTKPIPVAQR TLSFVCVPYG GGSAIVYQPL ADALPDGHRL
FAVAIPGHDI GLDEDALPFD ELASRCVEEI LRKVDGPLAV YGHCGVGSAL AVEIARRLEA
AGRRLEALYI GAIFPFARPE NKVLGGLSRV ARLERFRSDR GYANWLLSMG VDMSDIEPEQ
ATHIIQNMRK DSQSAEDYYT GLLRDSVDRL RAPVITVAGD RDPTTDFYAE RYREWHFLTD
TSAVVVLDEA GHFFLKYRAE ELAAIVTETR PALETPEPLS RQERGADAGW WLHGVSRSRE
RVVPTGPTPS MRRFLAVASG QLVSMTGSAL TEFAVPLWIY LHTGSLFRFA LFAVCGLVPG
MLAAPLAGAV VDRSNRRRVM LLGDTFAGGT QLILGILLWT GHLQIWHIYP LLICLSVSLT
FQRLAYGSSV AQLVPKHYLG HANGVVQMIN GVAQIMVPLV AVGLMAAIGL GGILVIDVAS
YAVAVAVVLA VRFPATMAWR RKETLLAEIA EGFRYSWGQP GLRAMLLFFA ALNVFLSPLF
LLISPLVLSF TTLSRVGEVA LAAGIGATLG GLTMTFWGGP RRLRMRGMLL CTLALAAFCL
VTGLRPTLWL IAVGAFGMSY WLTVVNGIYT TIVQVKVAQR FHGRVFALNT LIAWSTLPIG
WGLIVPYGTK LFQPHIGRMY PVLAAGMVLV VLAALRTPAL RRFDIDVPDS VPDDLIGLEA
RQRRPRTAEP AIPAELTEPV AEPAAGSVR
//
