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Database: UniProt
Entry: A0A0W0YVY5_9GAMM
LinkDB: A0A0W0YVY5_9GAMM
Original site: A0A0W0YVY5_9GAMM 
ID   A0A0W0YVY5_9GAMM        Unreviewed;      1967 AA.
AC   A0A0W0YVY5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Non-ribosomal peptide synthetase/polyketide synthetase {ECO:0000313|EMBL:KTD60814.1};
DE            EC=5.1.1.11 {ECO:0000313|EMBL:KTD60814.1};
GN   ORFNames=Lsha_1531 {ECO:0000313|EMBL:KTD60814.1};
OS   Legionella shakespearei DSM 23087.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD60814.1, ECO:0000313|Proteomes:UP000054600};
RN   [1] {ECO:0000313|EMBL:KTD60814.1, ECO:0000313|Proteomes:UP000054600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD60814.1,
RC   ECO:0000313|Proteomes:UP000054600};
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   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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:KTD60814.1}.
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DR   EMBL; LNYW01000043; KTD60814.1; -; Genomic_DNA.
DR   STRING; 1122169.Lsha_1531; -.
DR   PATRIC; fig|1122169.6.peg.1762; -.
DR   eggNOG; COG1020; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   Proteomes; UP000054600; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0047462; F:phenylalanine racemase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
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; 1.
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; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR036736; ACP-like_sf.
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; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:KTD60814.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1049..1124
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1142..1549
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          647..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1967 AA;  219366 MW;  FE933703DBB3681C CRC64;
     MLDTMTLKAE AGEQLIWNRL LQNPEDKSCT LSYRFLINQV LSHEQINAAV YSLLRQHPEL
     NYRFYAHDGV LYKRLHQPSL NPVTRIDGHS LVEKVLFCET LNPLYCFQWQ VQEGGFYLYV
     HLSHLIIDGS GFALLVSELE AAFSGAQKSH SELGSLDTAD KPRYGGVSHH LIAVSKATGD
     ALDTPPSRGL STGSRNLASD LDPWIPRTSR GTVECQDALT ATNLSDTPPS RGLSTGSSNL
     TSDLDPWIPR TSCGTAESSY WQEYLQGQSL YQSLPFLEHG GQEVLVHYEL AIQPELVKQI
     GEYRKNNKAT LFHLISTALA ITLHHYIKDE DLETTIRLAY YVKLNKKLDK FGCDINLLPL
     FVPCNEQASL QQILQTVIAV RSEQKERQHT PLAELLPYLD PARNTNLPLM NVVINESPGL
     LPQVTSGFIS EATGIENHSA ATTLSLVYAF DGEHLRLQFE SAQSMGLQVL LRQLASHFEQ
     VLTILVTQPQ TLLADLLFRE PFAPVCQGES FTYEKDTLWD TFARQMHEHQ TRIAISDEQH
     SLSYEQTHSI ITAIYEQLQP LDKEELANGI AVFLSRTALL PLAMLAALMA RVTFIPVAEN
     IPEGGRHAIL NETKSQIIFV DNQSEALLSA TEKETLRVIN IESELRNPSR DRQEAEPLDI
     RINKGINTDA SNPSAPSRSR LGLDQKILPL LQNDIAYILF TSGSTGKPKG VMITYDNLTN
     FLYSVSSNPG FTQHDRMLAL TSISFDISIN ELLLPLFCGG SVFVAANSVR SCHKSLGNRL
     NQEYVSVLQA TPSTLSLLMQ SGWVWHNKNK LRLWIGGEAL TADLVRFFKG QNIDIYNMYG
     PTEATIWVSA TQIHSPDVLS IGRPLANTSL YVLDKHGQAM PLGIPGELVI EGDLVGMGYI
     NHPSTSFKQS DSGLRRYHTG DKVLALANNT LLYLKRYDDQ VKLRGYRIEL EEINQQIRTL
     VPHFIGLTLA LYEPEPHLCV YYTSPADLNV AQLKAQLQRV FPEYKIPQRY QLISAMPLNN
     NGKIDRKRLM EAKRDDVPVA AELSRHKSSE WNPAEQQIVA LIAQHFAVTI TSRDHSLLDY
     GFNSLSFNQL SLLCDKELGL TISSHQFYHL NTLNKLAQYY VLNKSIHTPI TAPASSGQIQ
     AHMPVAIIGY DAVLPGGKTP AEFWHLLINQ ECLISEHKRP WLHGRERAAY VRDIECFDRK
     FFNLSPIEVM HMDFRQRLLL QCAFRTMEHA GIPFNSQSPQ QIACFIAATG MDSLLASAKQ
     EIPAHPYTLS GNSLSMLANR LSFYFNWQGP SVTVDTACSG SLAALARGVE CLALGKAEQC
     FVGSANLIID SEFTSALQAG RFLSPQYHCA SFSDQADGYV RGEGIFGFLL KPLDKAIRDG
     DSIHAVIHQV SENHGGRAAS LTSPSQQAQT SLLTAAYTPQ LAQQLSYIET HGTGTKLGDP
     IEIDALKEFE RLSLAKNSHQ AVYLGALKQN IGHLEASAGF ASLLKVILAM KHKCLPANYN
     NGLLNPLIKW DNSKLKLLTE TIPWEHESLT AGISSFGFGG SNAHVVLSHH ADNKLRSDSD
     ETALPILLSA KTRNALRARI ISLLGDLAED LCFKDVAYTL AMGRTHFDCR TAVVAKNRQE
     LVRKLNDLLH TEDLRSSLET DGVLDDYLAG KNCDWQPVFA ALDCKRISLS PYVFDAEPCL
     HELFQHSSDL DLMADLGWLK ISEHQRKITL SKNHPFLAQH QVFNNRVLPG VTYIDFLLRE
     LRQQRPEQNS FCLENICWLQ PAVCEGDSLT LILETIQHQD AITFQFCNSE RQVLATGQYT
     ELKQDYASLY SWFEPSRNEL KRVGLDTVAA DAVYKKFSQL GIDYGSYFQG ISSVTLYENM
     ALTRLALNPQ GGCTALLDAS FQSGMAINLA ESLPGLMPFS LGKMIIFNHS KLIRLEKAFV
     YTLKNSPFRT NFIICDEQDE PIVALIDLGV KPSQLKFTGV VARISEA
//
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