ID A0A095UVY0_9GAMM Unreviewed; 1307 AA.
AC A0A095UVY0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Enterobactin synthase subunit F {ECO:0000313|EMBL:KGD78478.1};
GN Name=entF {ECO:0000313|EMBL:KGD78478.1};
GN ORFNames=HA49_03660 {ECO:0000313|EMBL:KGD78478.1};
OS Tatumella morbirosei.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Tatumella.
OX NCBI_TaxID=642227 {ECO:0000313|EMBL:KGD78478.1, ECO:0000313|Proteomes:UP000029577};
RN [1] {ECO:0000313|EMBL:KGD78478.1, ECO:0000313|Proteomes:UP000029577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 23360 {ECO:0000313|EMBL:KGD78478.1,
RC ECO:0000313|Proteomes:UP000029577};
RA Smits T.H., Palmer M., Venter S.N., Duffy B., Steenkamp E.T., Chan W.Y.,
RA Coutinho T.A., Coetzee M.P., De Maayer P.;
RT "The draft genome of the Tatumella morbirosei type strain, LMG23360T
RT isolated from pineapple rot.";
RL Submitted (DEC-2014) 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: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
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:KGD78478.1}.
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DR EMBL; JPKR02000005; KGD78478.1; -; Genomic_DNA.
DR RefSeq; WP_038016905.1; NZ_JPKR02000005.1.
DR STRING; 642227.HA49_03660; -.
DR eggNOG; COG1020; Bacteria.
DR OrthoDB; 9757559at2; -.
DR Proteomes; UP000029577; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; 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:1901362; P:organic cyclic compound 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 Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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 InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
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; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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:UP000029577}.
FT DOMAIN 977..1052
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1307 AA; 144231 MW; 78133650EB7D5E51 CRC64;
MSEQTRWLPL VAAQPGIWLA DQLSPYTNAY AVAHVTELRG EISLPHLSAA IRHGLAEADT
LHMVFEDIEG EAMQCPGQAP VIDAEYRDLR AETDPRETAE YLIHQDLHSD LRLAPGKPMY
RHLILQIEDN HWLWYQRYHH IAIDGFSFTA LTRRIAEIYT ALCQQNDTGP TPFTPFSDVV
AEYLDYQQSA GWQRDAGYWQ EKVNTLPAPV SLSEQPLSGQ PPSTELIRLQ LTLSATDLQP
LCNQLTAEKL TLTDGAIALV AVWLARLTGQ QPFSSGFIFM RRLGSAALCA TGPVINVLPM
AVDYQPGLTL TELAARLAKE IKKNRRHQRY DSEQVMRDAG RHGDSDPLYG PVINVKMFDY
QLSFNGLHAD TRHLASGPVR DLEIAIFPGE SGDVTFGILA NAGRYDAGQL QEHLDRLPLL
AQQFGQSAGL ICSEAIMLNA KEQQQLADIG QARHPVPATT LSDLLEQQAL SSPQAIGLTD
VHQQLTYHEM HQQVLALAQQ LHQAGVSRGD IVAVALPRSV CLSLALQAIV RLGAVWLPLD
TGYPDDRLQM MLEDAAPKLL ITGYELTSRF RAISEVAQYH YNALLSPLCG PLSLPGPLAG
DGAYLIYTSG STGRPKGVLV SHQAIVNRLL WMQNHYPLNS TDVVLQKTPA SFDVSVWEFF
WPLITGARLM MAPPESHRDP EALLRLILDY HVTTLHFVPS MLAAFTSSLP PDSARLVARE
LRRVFCSGEA LPTALARQWQ QLCGTELHNL YGPTEAAVDV SWYPAFGPEL AAVTGSSVPI
GFPVWNTGLH ILDGQLQPLP QGIAGELWLS GIQLAQGYLG RPGLTASRFV ALPGAEGERM
YRTGDVVRRL ANGAIEYLGR NDDQLKIRGQ RIELTEIDHV LLEQAGVEQA VTLARVLQEN
QSHDQRWEDA RQLISYVISD QPVDTEQLRS QLAAHLPAHM VPVAIMQVAE FPLSNNGKLD
RKALPLPALH SGKHQRKPTA GLESELAEEF AAILGCDTVF ATDDFFALGG HSLLAMRLAA
RLRKKLHQHI TVGQIMVAPS VEKLARLLTA PQQDQGNEAG HEPLLPLRES HGPRLFCFHP
ASGFAWQFSV LRRYLAAHWS VTGIQSPTAD GILQQSQHID DICDAHLQLI RQQQPHGPYY
LIGYSLGGTL AQGVAARLEA AGEQVAFLGL LDTWPPETQN WDERQGKNVL DPEVLAEVDR
EREQFMQSQR KMAGEDMAGM FEVISQNYAS AVRLLTTATS AHFGGKATMF LAERTRLQGA
DAQQCWAPYI RQLEVVPVDC AHSEIFSEGV LAIIGPAISQ RLESLQK
//
