ID Q748H3_GEOSL Unreviewed; 1136 AA.
AC Q748H3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=[acyl-]glycerolphosphate acyltransferase and acyl-(Acyl carrier protein) ligase, major facilitator superfamily domain-containing {ECO:0000313|EMBL:AAR36421.1};
GN OrderedLocusNames=GSU3029 {ECO:0000313|EMBL:AAR36421.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR36421.1, ECO:0000313|Proteomes:UP000000577};
RN [1] {ECO:0000313|EMBL:AAR36421.1, ECO:0000313|Proteomes:UP000000577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA
RC {ECO:0000313|Proteomes:UP000000577};
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AE017180; AAR36421.1; -; Genomic_DNA.
DR RefSeq; NP_954071.1; NC_002939.5.
DR RefSeq; WP_010943656.1; NC_002939.5.
DR AlphaFoldDB; Q748H3; -.
DR SMR; Q748H3; -.
DR STRING; 243231.GSU3029; -.
DR EnsemblBacteria; AAR36421; AAR36421; GSU3029.
DR KEGG; gsu:GSU3029; -.
DR PATRIC; fig|243231.5.peg.3054; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_008489_1_0_7; -.
DR InParanoid; Q748H3; -.
DR OrthoDB; 9799237at2; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd05909; AAS_C; 1.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR CDD; cd06173; MFS_MefA_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; IPR042099; ANL_N_sf.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50850; MFS; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:AAR36421.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:AAR36421.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000000577};
KW Transferase {ECO:0000313|EMBL:AAR36421.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..408
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 1136 AA; 121122 MW; F30FD2C6FFC4C006 CRC64;
MNSTDTGTDT LPSSFKRLNL AQALGALNDN VIKLIIVFFL ISHFGQERAA TVAAIGSAAF
VAPFLFFSAL AGSLADRFPK GWIIVRVKAL EVGIALLAVA GLLIASPLLL GAVIFLLGTH
SALFAPAKYG VVPELVAREE LSRANSLLEM WSFLAIVGGT ALAPFLVQLA GGRHGVALLA
GVAVALCGLL VARTLPETSA AAPERQVVLS PAAYWRTLRS LKHDGYLLLA VLGAAYFLFV
GAFCQLNLLP YGMKLLGLPE EQSGYLFVAA AVGIGVGSLL AGRLSGRTVE FGVVPIGAAG
LTLCSFLLAT LPAHLPSVLV AVTLFGMSAG LFIVPLQSFI QLRAPADRRG EILAASTFLS
WVGVLLASAL LWTLTGPLGI SPAGCFGVLG AITLVLTLAT LRVLPDFLLR FVALVAMRLC
YRLAVIDDRH VPVEGGALLV ANHVSWLDAL LLIATQQRRI RFVMEREIYR TPVLKQLCSL
MGVIPVSSKD GRKGLLEFIA SARGALDQGY LVCIFAEGAI TRNGMLNQFK GGFERIVRGT
SHPIIPVYIG GAWGSILSYA HGKLLSRFPS LLPYRVTVLF GAPLRAGSSV HDVRRAVMEL
SCAWFQTRKS RRRPLGELFA ETARENWHRL AVADTGGREL TYGRALTGAV ALAARLKPFT
AGQEMAGVCL PPTVAGALVN LALTLNGTVP VNLNYTASAD GIRSSLDQCG IKVTITSRRF
QEKLGSLPEF PGVLYVEDLL AGLTGGDKCQ AFLKARFLPL RLLAGKAGFS ADQPATVIFS
SGSTGEPKGV MLSHHNIISN LEALRMVFRA TRRDNICSAL PFFHSLGFTG TLWLPLLSGF
SVVYHANPLD GETIAATVRE RRSTLLIATP TFLMAYLRRA KPEDFASLRL VITGAEKLKP
KLADSFQEKF GIRPMEGYGA TELSPVISLS LPDVEIDGVR QAGFREGSVG LPVPGVVVKI
VEPETLEPVA EGVTGLILVK GPNVMLGYLG KPEKTAEVIR DGWYVTGDLG YLDDHGFLHI
TDRLSRFSKV AGEMVPHGAV EDALHVRLGQ AGLVAVTGVP DERKGERIVV VYTPEAGDAE
TLHRFMTESE LPNLWKPARD CYVAVETLPV LGTGKLDLRG VRAVALAAVG LGGGSV
//
