ID   U2QVP4_9FUSO            Unreviewed;       826 AA.
AC   U2QVP4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Putative acyl carrier protein {ECO:0000313|EMBL:ERK66955.1};
GN   ORFNames=HMPREF1984_01256 {ECO:0000313|EMBL:ERK66955.1};
OS   Leptotrichia sp. oral taxon 215 str. W9775.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=1321779 {ECO:0000313|EMBL:ERK66955.1, ECO:0000313|Proteomes:UP000016640};
RN   [1] {ECO:0000313|EMBL:ERK66955.1, ECO:0000313|Proteomes:UP000016640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W9775 {ECO:0000313|EMBL:ERK66955.1,
RC   ECO:0000313|Proteomes:UP000016640};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC         CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00024484};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000256|ARBA:ARBA00024484};
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:ERK66955.1}.
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DR   EMBL; AWVR01000050; ERK66955.1; -; Genomic_DNA.
DR   RefSeq; WP_021766542.1; NZ_KI272838.1.
DR   AlphaFoldDB; U2QVP4; -.
DR   STRING; 1321779.HMPREF1984_01256; -.
DR   PATRIC; fig|1321779.3.peg.1189; -.
DR   eggNOG; COG0204; Bacteria.
DR   eggNOG; COG1022; Bacteria.
DR   HOGENOM; CLU_000022_45_1_0; -.
DR   OrthoDB; 9778383at2; -.
DR   Proteomes; UP000016640; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR002123; Plipid/glycerol_acylTrfase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   PANTHER; PTHR43272:SF52; CARBOXYLIC ACID REDUCTASE; 1.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016640}.
FT   DOMAIN          527..603
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   826 AA;  94379 MW;  AFC9797BC9858D8A CRC64;
     MFLNRGDRLA IVDFEDRKIN YTELVNNVKY FSENVIPAEK EDFGLILMEN RPEWIYTYFA
     LWDRKAIPIA LDSTSSSKEI LYVLGDSDPK FIICSNESEK NVREAVSMYE KGEITVINVD
     NHPIDENKLE VIRNSNFELE NPEGDSIATM LYTSGTTGSP KGVMLTFNNL SSELEGLEKK
     DLLEPTDQIL ALLPFHHVLP LTATVLIILQ HQASMVFVKK IASKEILEAL DKNNVTALVG
     VPRVFKLFYD GIKQQIDSKF ITRTIYKLMT KVKSFKIRRK VFAKVHEKFG GKLTFIVSGG
     AKLDPEIGEF YETLGIYVQE GYGLTETSPV IAVNTKKDRR IGTVGKKLDN IEAKIVDEEL
     WVRGPIVMKG YYNKPEKTAE VITEDGWFKT GDLASIDEEG YVTIRGRRSS MIVLSNGKNI
     DPEKLENKVI EKSKKLIKEL GVFGHNDKLV AIIVPDLLEC RKQGITNIKA YVKNIVEDYN
     LTVHNYEKIL DYKLYEEELP KTRVGKVRRF MLPELYLKTN VKKKQVEEPD DEVYRMLKDY
     IKKLKGIEAQ PEENLELEIG MDSLDIVEFF AYVENSFGIH LDEEKFSEIS NLKALSEYIN
     EKATKIESGE VDWKKIIEAA PPVEEKNRWA TRVLRPLLDL IIKVYFRLKR VNRDKLSDKP
     QQIFVANHQS FIDPLVLGSL LPAGILYNTI FLAIDWYFKK GLMKLLVSHG NVVLIDINKN
     IKKSVEEIAA NVKAGKNVLI FPEGARTKDG KVAEFKKVFA IIAKELNVDV QCLGIKGAFE
     AYSRYMKFPK PKKIEVAVLE KFKPEGTYDE IVEKARNIIK DYVEGK
//