ID A0A0W0U4T4_9GAMM Unreviewed; 1408 AA.
AC A0A0W0U4T4;
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=Peptide synthetase, non-ribosomal {ECO:0000313|EMBL:KTD02853.1};
GN Name=tycC_2 {ECO:0000313|EMBL:SPX59947.1};
GN ORFNames=Lfee_0691 {ECO:0000313|EMBL:KTD02853.1}, NCTC12022_00658
GN {ECO:0000313|EMBL:SPX59947.1};
OS Legionella feeleii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=453 {ECO:0000313|EMBL:KTD02853.1, ECO:0000313|Proteomes:UP000054698};
RN [1] {ECO:0000313|EMBL:KTD02853.1, ECO:0000313|Proteomes:UP000054698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-44C {ECO:0000313|EMBL:KTD02853.1,
RC ECO:0000313|Proteomes:UP000054698};
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.
RN [2] {ECO:0000313|EMBL:SPX59947.1, ECO:0000313|Proteomes:UP000251942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12022 {ECO:0000313|EMBL:SPX59947.1,
RC ECO:0000313|Proteomes:UP000251942};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
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DR EMBL; LNYB01000021; KTD02853.1; -; Genomic_DNA.
DR EMBL; UASS01000004; SPX59947.1; -; Genomic_DNA.
DR RefSeq; WP_058443907.1; NZ_UASS01000004.1.
DR STRING; 453.Lfee_0691; -.
DR PATRIC; fig|453.4.peg.751; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000054698; Unassembled WGS sequence.
DR Proteomes; UP000251942; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12230; -; 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 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; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_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; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 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; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054698}.
FT DOMAIN 1090..1165
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1408 AA; 160875 MW; 4DB6AF35CBA78F87 CRC64;
MEITTCLIGE DSLVIQCGDQ LLSRNHRIHL VISPLNSVQE WAEEHGISWI ASIDKLANIE
PFQVDYLFSI VNSRILSKSI RNLARCYAIN YHDSLLPKFA GLNSTSWALV HNEKEHGVTW
HIMNDKIDEG EIVYQQSLPI YPNDTVLTLN LRCYENAISS FTQMIKLIEA GLLAPRKQVL
DKRSYFAANH HLPCFGFIDW RLFSAKTIER ITRALSIQKY SNHVGTLKLL ADRDYAIVSQ
VELGCAPNTA ENKLGTILDI DENGLVVSTV GQPIKFVELL SLAGEPISIK DWVNSHGLQV
GQVLPYYRVK DIEAQRKYHS SALANERYWI SKIKAISEHN TFNLQRLKQS MEFERLETSI
CLNDIFPSKQ FDNKVELLLT AILVYLYRLN NQEQLSVSIV QPEYNHLQEQ FGPLFSGFLP
LLFHKENDFS FQEALESVTK SLVELDKRSV FLSDIAARHP ELKGSQMESG IVINLSGANK
DYPCQTETVL YFNLDPDRGK IEILHRMELN RDDSLLKELM SHCTQHLVNI LIQLINYPFV
SARKFCFLTQ AERYNLLQVW GKGKTRYLPE KSLAMLFETQ VASNPDKVAV YFNHLSVTYL
ELNELAERVA NRIRQQQIPP QHFIGLYLQR SIEMLAVILG ILKANCAYVP LDTKYPLLKI
EQIVEDANLS CLFIQQKSVE QFNDFFKQKE KKVELLTIEA ILSTPQKACE QVPNGLTITN
KIAYIMFTSG TTGRPKGVVV THRNIINYCK WFTETTHFDE KCTIDFSSSI AFDLSVPCTL
APLLVGGAIA IATDVQKTNP QLYLTHLKKH QVTHAELTPG YLEMLLNYPE EVIDLVHLRY
LLLGADVVLS TDVKRWLSLC PHHQVINEYG PTETTVSVTS YFVNKDELDK GTSVPIGQPA
FNSTGYVLDQ YKNLCPFGVK GELYIGGAQV TKGYLNRPDL TQEKFIHVDF TKPDEVLYRT
GDMVCWLPGG SLQFFGRNDH QVKIQGYRIE LPAIESILVK FPGIHQAVVV VMRGKSKEAY
LRAYLVTDKK PKTSNELREY LAGYLPGYMI PREFCVIKSI PLKENEKIDF TSLERQGFQL
LRFNEQDTID ALTPHEKEIK GIWEQIFHRK VHSTQEDFFA MGGDSLTALQ LISTLKTHYN
LNFPLQLVFE YPTISSLATK IEEFLASKRS EKHFSIKANP LIKLATGKDE SPLFLVHPVG
GSVFWYKQLA SYLHGKYTVY GIQDPNLDGM LLRFNALEDM ASFYLQEIKK VYSGDQYCLG
GASFGATVAF EMAKQLVHEK KSIRFLGLFD GWAHYPHDLM QEDSSTFLSR TEANQATINN
KTKESLYELE QYRKTLLLNY KLSSLRADVT LFKASELWPS FKLIDDFNNG WRPYVEGEIR
QYAISGNHET MFFEPYVQRL VECLSMKI
//