ID L1MZ42_9BACT Unreviewed; 1045 AA.
AC L1MZ42;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:EKX96563.1};
GN ORFNames=HMPREF9151_02409 {ECO:0000313|EMBL:EKX96563.1};
OS Hoylesella saccharolytica F0055.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1127699 {ECO:0000313|EMBL:EKX96563.1, ECO:0000313|Proteomes:UP000010433};
RN [1] {ECO:0000313|EMBL:EKX96563.1, ECO:0000313|Proteomes:UP000010433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0055 {ECO:0000313|EMBL:EKX96563.1,
RC ECO:0000313|Proteomes:UP000010433};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EKX96563.1}.
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DR EMBL; AMEP01000156; EKX96563.1; -; Genomic_DNA.
DR AlphaFoldDB; L1MZ42; -.
DR STRING; 1127699.HMPREF9151_02409; -.
DR PATRIC; fig|1127699.3.peg.2210; -.
DR HOGENOM; CLU_003055_0_0_10; -.
DR Proteomes; UP000010433; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR InterPro; IPR004869; MMPL_dom.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF03176; MMPL; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:EKX96563.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010433};
KW Transferase {ECO:0000313|EMBL:EKX96563.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 645..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 736..753
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 810..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 878..987
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1045 AA; 117652 MW; 540531F1A5A34F86 CRC64;
MITRALLRIY DYLHTHRYLR FLLLVTLLAA AVISALQLRF KEDISDFLPD NDTYHRSMDV
YRQINAADRI FVVFQMSDTT QTDIDRIVEA VSIFETQAQQ KHWQITARID YDEVLGVADF
VYANAPLLMN EADYTRMSRR MCTDSIAAAL QKDKEMLLFP SGNLLSQNIQ RDPLGLFTPI
LERLQTSGRA MRYELNDGYI FAPDNRFAIV MIDSPYGSSE TDKNGKLIAG IDSVARTIEA
KLGNVQITAT GAPVIAVDNA QQIKTDSVWA IGIAVVLILC LLVYTLRRVR YLSLIAVSLG
FGWIVAMGAI ALVSREVSVI VLGIASVIIG IAVNYPLHFV SHLGHCSSPR DTLKEIAVPL
VVGNITTVGA FCALIPLEST ALRHLGLFAA FMLVGTITFV ILFLPHLCGR VANRCSASET
VVDKAEETPF NPVYPKNKYV VAALVVVTLV LGYFSLSTQF DTDMQHINYL KPKQKALLMD
LGRMRNEQPG TTQVYFATSG ANVEEALERS AHAFSDLLIP GKQEQRRRID RWNKFVTQYR
QLLTQQLTAE AVRNGFTPDA FEDFNRVVNA RLQPQDLAFF SPLTRNGLGN RILGNTVVNV
VNVPSAQADS VVMAFNGASG AQQWAFDVQS MNATIATTLS QNFNYIGWVC GIIVFVFLWI
SFKKFEHALI AFLPMAVSWL WILGTMHLLD MRFNLVNIIL ATFIFGQGDD YSIFITEGLI
YEQTYRRRML ASYKRSIFIS AAIMFIGMGS LIIARHPALR GLGEITIVGM ASVVVLTYII
PPMLFGWLYT DKNGAERPQP ISFSRLLVTI YASGIYLFQV LYGCVLGTWL FVLHRKTPSR
MAFFHRQKHL FFHFDIFHIP GVKTRICYDE PEDFKRPAVI ICNHQSILDP VCLMALSPKI
LISIGRKVWH NPIVSPVLRF SDFIPVENGS EAIVDRCRKH IKNGYSIAIF PEAERVISPD
IGRFHNGAFM LARELNVDIL PVYLHGLREL MPRHSIVCNR GTLTIRVGKR ISQQQIQQMG
NSILEIKRAV YKLYTNEYEG QKENV
//
