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Database: UniProt
Entry: A0A1H7WKM5_9BACT
LinkDB: A0A1H7WKM5_9BACT
Original site: A0A1H7WKM5_9BACT 
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
//
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