ID A0A1H7WKM5_9BACT Unreviewed; 1282 AA.
AC A0A1H7WKM5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferases {ECO:0000313|EMBL:SEM21447.1};
GN ORFNames=SAMN04488505_103687 {ECO:0000313|EMBL:SEM21447.1};
OS Chitinophaga rupis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=573321 {ECO:0000313|EMBL:SEM21447.1, ECO:0000313|Proteomes:UP000198984};
RN [1] {ECO:0000313|EMBL:SEM21447.1, ECO:0000313|Proteomes:UP000198984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21039 {ECO:0000313|EMBL:SEM21447.1,
RC ECO:0000313|Proteomes:UP000198984};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOBB01000003; SEM21447.1; -; Genomic_DNA.
DR STRING; 573321.SAMN04488505_103687; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000198984; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR004869; MMPL_dom.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33406; MEMBRANE PROTEIN MJ1562-RELATED; 1.
DR PANTHER; PTHR33406:SF2; MEMBRANE PROTEIN SCO6666-RELATED; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR Pfam; PF03176; MMPL; 2.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:SEM21447.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198984};
KW Transferase {ECO:0000313|EMBL:SEM21447.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 688..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 756..774
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 781..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 898..1007
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1282 AA; 145172 MW; D32715163E9149C0 CRC64;
MGSFFVHIYN FYATRKMWLW ISVVAAFALT GYFASRIQLE EDITKILPQD KTLNKLQQVF
NDSRFADKLV VMVSQKDTAG AAEPDSLTTF AADLEVAIKE DTALSSYVKQ VQAKIEDTAI
LGLMATIQQH LPVFLDEKDY RTIDSLIQPE RLHQTLEHNY QTLISPAGLV LKKMIQADPV
GMSWQGVKKL QQLQIDDQYE LYDGFIVTRD HRHLLLFLTP AYPPSATGKN AVFLKLLQAK
LAEMQTGHTF TAASYFGATA VSEGNAHQLR MDTMLTQGIG VVLLIVLIAL FFRKKRAPVL
VMLPVVFGAL FSLACIYLIK GKLSVIALGA GAVVLGIAVN YSLHVFNHYR HLGNIRETIR
DLATPMTIGS FTTIGGFLCL QFVESPMLKD VGLFAALSLV GAALFSLIFL PHWILTKQPV
AAHSHTWLDK LASYRPEKNK YLVFGILLLT VIFCFTAGKV GFESDMMRMN FMTPELKAAE
AKLNSLSAYA AQSVYVVTEG RTLEEALQAN ERMLPVVQQL QQQGIVKRYA GVGSLLLSQQ
EQQARLQRWQ QYWTPQKKQQ LITYLQQQGP AAGFKATAFD PFAQWLQQNF TTMTAADQEA
LRNSSLGDYI TVKPDRVSLV TLLKVNPGQK KAVYKALAAQ QNTTVLDKQY AANRLVEVIR
NEFNSIAWMT SLLVFFALLI SYGRIELALI TFIPMLISWI WILGIMGMFG IRFNIVNIIL
STFIFGLGDD YSIFTMDGLL QQYRTGKEQL SSFRSSIFLS AITTILGLGV LIFAKHPSLR
SIALISMIGI GCVVLISQVM IPLLFNWLIA KRTRRGWAPW TLSGWCISVF AFTYFTLGSL
LLTTVGYILI RLNPFNKQKG KYLYHVFLSW FTWSQLHIMG NVKKRVINPL NEQLEKPAVI
ISNHQSFLDI LISIALNPKV ILLTNEWVWR SPVFGAVVRL AEYYPVAEGA EASVDKLRGM
VEQGYSIVVY PEGTRSPDPV IRRFHKGAFY LAEQLGLDVL PVLIHGTAYT MSKSDFLLKN
GVLTAQYLPR ITPEDKSWGE GYAARTKSIS RYFKQQYEAL RRSVETPAYF REQLIYNYIY
KGPVLEWYMR IKTRMENNYT LFHSLVPEKG RILDIGCGYG FMSYMLHFLS AERTVTGVDY
DEDKITTANH CYLKNDKVNF EYADVVNYTF EQHDAFIISD VLHYLQPQEQ EQLLQRCLQQ
LAPGGVIIVR DGDADMSKRH EGTRLTEFFS TRLLGFNKTK QQLSFFSGQH LKQLIEKMGA
RLEQIDNTKY TSNVIFVIRQ KA
//