ID A0A0W0WYR1_9GAMM Unreviewed; 3158 AA.
AC A0A0W0WYR1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Type I polyketide synthase WcbR {ECO:0000313|EMBL:KTD37472.1};
GN Name=rkpA {ECO:0000313|EMBL:KTD37472.1};
GN ORFNames=Lnau_0662 {ECO:0000313|EMBL:KTD37472.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD37472.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD37472.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD37472.1,
RC ECO:0000313|Proteomes:UP000054725};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD37472.1}.
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DR EMBL; LNYO01000011; KTD37472.1; -; Genomic_DNA.
DR RefSeq; WP_058503732.1; NZ_LNYO01000011.1.
DR STRING; 45070.Lnau_0662; -.
DR PATRIC; fig|45070.6.peg.706; -.
DR OrthoDB; 5657178at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000054725; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046483; P:heterocycle metabolic process; IEA:UniProt.
DR GO; GO:1901360; P:organic cyclic compound metabolic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 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; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR013120; Far_NAD-bd.
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; 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; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054725};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..415
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1615..1696
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2710..2785
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 3158 AA; 355502 MW; C03AB31E3D015C60 CRC64;
MKQHSPISII GMACEFAGQA DSLANFYKVI LEGVDATSDI SEGRWNVDLD SLPQSIRHGG
FLKRNPWSFD AQFFAISPKE AAHMDPQHRI LLEQTYHALE DTNLDLDTIK GSNCGVFIGL
GTQDYSRIMH NSGQFSGLHS KGSLGSMAAG RIAYHFDLIG PNFVVDTACS SSLVALDQAV
KALQDHRCDL AIVGGVTLIL TTDYNTDLAS ANLLAKDGRC KPFSKGADGF ARGEGVGVII
LQRRQEALRD KRRIYANILG SAINSDGKTN GITAPSKESQ KRVIQDALKD AQISAQEVNF
IETHGTGTDL GDKIEFAALI EIYQGREEPL YIGSVKGNIA HCEAAAGIAG VIKTSLCIYH
DLIPPHTAAN FLNPDLRVAS LKAQFPAQVL PKRNIVGTVS SFGMSGANAE VVLADEPTKN
AAASADCPQV YPYLLLSAKS AESLHKLGSE YRLLLEHCEE EAFNKCLSQA NLRNNCSGYR
KLVYGQDKTA LLKQLDKIDL TALKKRMVKG KTKFAFMFTG QGAVFKEMTR VLYDRIPLYR
NILNDYAAKM DDVIHLPHKI ISYIFNDEFS LSLDDPQTAQ LSLFLIEFSL ARLLNLLGIT
PDFVVGHSLG EYAAACSAGI LSFEQAVQMV NLRSQAIKEE PGLQDGLMLQ IYATNELVQK
LLAELRLKNP LLALWISVNN APEIQVVSGN KESVLQLTDL LKQKGIPYLK LNTSHAFHTP
CLELAATNFK DRALASAMSF TLKNSITSFI STAEPHRDDN QNQAFASIDY WAAQIVKPVR
FVDAIESCYE LGVRSFIEIG PDSILTNLAR QCLKNKESSA ELEFIAMNSK NKNNLDSLFS
VLNYFYSTHR LDGSKLGLLD DKQRVFSSFF LPVYPFARVE LLPDYLKNSR VPAVIEKNNS
KKIRLEPTHL EFQINLDLSQ IEHAYIAQHV IHEMCILPGS YYIATSIQLL ETFKESYLAN
QPQTIIELDN LLIMHPVIIS QSGQESLKVT IHQQKPNQYK FSYFCLAEID QLVCEMTLLL
KSYEEPNCVE INQGTKIQDT SEFYSNYAVC GVNYGPLFKK QKSYYNLDSQ NIISELEAAE
GYFTSHAAFI DNCFQTMALG LNQLGSAFAP TAVNQFKFYK EEKWGVGLGC HAQIIEQKEG
HLEANLKVYN AQNKVVMEIN GIVCKSIQLD ALSANVIHKV ALEKIAVSAP DNSLKDFAFL
ANFKTEWVKP ESILAWSDLQ AKTTIDVRHL IIGFDGLAWD KNELFSLFQC LFNFLRLQAE
KISGNLKVIS FLSLNDKAKD YKKLLAPLLK AMTLAFPTEF PNLSFRHFSY TKLTKDNIAF
LFAEDKELPT DHEFLIPFWE VYGNELYRYK TIPQKPNQAE PLPKEGYYLI TGGLGGIGKT
LVRHMVSNLG CRNLILTYRK LEPEAEQFIT ELNDQYDANI RCHHVDLRSE SQLVKLFATL
PRPLYGIFHL AGIIQDQSLA KTSPHSIENV LAAKLFSAWT LHELSQEITE LKAFVLFSSL
ATLISSPGQF NYALANLGLQ ELAAHRKNSH LPVSLIDWGP WANIGMMANS DSLSASSIVL
SKFVPLSPTI CHEALFSCLN QTNDSHFAVF KMNKREPIVR TSVESETKIS LNPHSSKKEA
AQFIKALLLR LIAQETNHAS ASIDEHLILS ELGLDSINTI RIRAELQTEL NLAIPLSILL
EETTLERLVD QVLVLWLANQ NNQNQHSESN EEASVNRGDA NFFSLSYNQF SIWYEQHAIE
NNQAYHCSIG WKIRGGDLNL KQVYANWEVL ISRHEMLRAL FSSREGNLGY ELLSVSQALE
QQMVVVETIE ADRDPQQYLQ NYLLRKIDFN RELPTKVLIL SHQNDVYLML SSHHIVMDAA
AMFYLGKKLL TSLCEADYVL DKDFSSQPYH EFTKQQFLQS AEFDLKTLSF LRKEVLNEEG
ELRVFELPKK SNTGILNLAK GATKTILFSE MEMQIIQSLP ASIRVHLCLS AWALLLAKYS
GEENLLIGVA FNGRTQKKWT EVVGHFVNVL PLCIKVNQHQ ASNQFINEIK SRLIELLEFQ
DFPLVKLMKD PEVKQALQGR PLLQTYFNYF DASDLDISVN NQLVTIDALV YPQQEAQFEM
SLWVTRTSRG FDFEVKYQRE LFSETMLEKL VGYYKTVLIA LSQALLQSNT QLKLAEIQFL
SETELAKRLP PESTNRPSQL VYNYFAEQAA SLPQSVAIEM REQNISYQSL QGWVDELALA
LTEFPQSKDE TVAIIAPERA NIEFIVTVLA LWKQGFAFVP LNSHHPFERI KYVLDTVGCR
KLILVDVLSP NLENYICTNN KLLLEVRIEF PQLQIQVLNE SIPEENDRFE NRSQANPSDL
AYILFTSGST GLPKGVLIEQ EGLIDRLLWM KNYFNFSAAD KFLQSTLLTF DVSLPEYCLP
LICGATIVLF HPEESQNAHA ALCTYHQVTM MSTVPSLFSI LLSDLAGCPT LKHLIMIGEV
LPRAIVNKWL ASNQTCTLYN LYGPTEVTVY ASAHACREPI NSALVPIGEA ADNVIPLVLD
QYGNPVLDEV IGELYLAGSG VARGYIGGQL KSDPFINNPW QSLHYTRMYK TGDFVRWLEG
GRLEYIGRKD NRIKLNGLLV ELGEIEERVL KAFPDLENAC AIITEFKIKE TLIKHIVLCI
MPECTDSSII MEHLKQHLPQ YMLPWKIISY AEFPRNSSAK VDRKLLTNLV KELYEEESVQ
AKLRPKSSHQ PVTFMEKEIC KIWETLLQKS NLGIDENFFE LGGDSLLLTQ MILLVEKQLG
IKTNFAKFLA NPSINSLLHG LSMESPIWEN EFKLLKAISP YQEVKKTKAV LLTGGTGHLG
IHLLRSLLNQ TDKQIYLIIR AESKTKAIER LTERYFSVFG DSLALNRLCI YSGDLALLNF
GLEEADFQKL CQEISLIIHA AAEVNHVVDY VRLKKSNVLV SKNMLDLARS AHCTHFFHIS
TQFSELSILP ESYMNETSIN EFSSGYEQSK FIAESLMSAA KNLKYPVTTL RLPLIIDDSD
PLLLRQNHFV AFVMKCLRLG AYPDIGLSFA LLATADLADF VAELSNKSYL EPEVYNCHTR
RISLQELFDF FITETEYKVN KLEPSLWKAR VLESTYETDP FYKLLPLYTS SLLISENVNE
QLIEHKGFLK AIETTKLAVT DNAHIKKIGS MLANYSRL
//