AAS_YERPE
ID AAS_YERPE Reviewed; 718 AA.
AC Q74RZ6; Q0WIP0; Q8CZY1; Q8ZHU1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Bifunctional protein Aas {ECO:0000255|HAMAP-Rule:MF_01162};
DE Includes:
DE RecName: Full=2-acylglycerophosphoethanolamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE EC=2.3.1.40 {ECO:0000255|HAMAP-Rule:MF_01162};
DE AltName: Full=2-acyl-GPE acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE AltName: Full=Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE Includes:
DE RecName: Full=Acyl-[acyl-carrier-protein] synthetase {ECO:0000255|HAMAP-Rule:MF_01162};
DE EC=6.2.1.20 {ECO:0000255|HAMAP-Rule:MF_01162};
DE AltName: Full=Acyl-ACP synthetase {ECO:0000255|HAMAP-Rule:MF_01162};
DE AltName: Full=Long-chain-fatty-acid--[acyl-carrier-protein] ligase {ECO:0000255|HAMAP-Rule:MF_01162};
GN Name=aas {ECO:0000255|HAMAP-Rule:MF_01162};
GN OrderedLocusNames=YPO0793, y3181, YP_2864;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Plays a role in lysophospholipid acylation. Transfers fatty
CC acids to the 1-position via an enzyme-bound acyl-ACP intermediate in
CC the presence of ATP and magnesium. Its physiological function is to
CC regenerate phosphatidylethanolamine from 2-acyl-glycero-3-
CC phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or
CC degradation by phospholipase A1. {ECO:0000255|HAMAP-Rule:MF_01162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP]
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP];
CC Xref=Rhea:RHEA:10304, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:64612, ChEBI:CHEBI:65213,
CC ChEBI:CHEBI:138651; EC=2.3.1.40; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain
CC fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01162};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01162}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01162}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE
CC acetyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01162}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ATP-dependent
CC AMP-binding enzyme family. {ECO:0000255|HAMAP-Rule:MF_01162}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM86731.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL19465.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86731.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS63046.1; -; Genomic_DNA.
DR PIR; AG0097; AG0097.
DR RefSeq; WP_002209843.1; NZ_WUCM01000007.1.
DR RefSeq; YP_002345848.1; NC_003143.1.
DR AlphaFoldDB; Q74RZ6; -.
DR SMR; Q74RZ6; -.
DR IntAct; Q74RZ6; 2.
DR STRING; 214092.YPO0793; -.
DR PaxDb; Q74RZ6; -.
DR EnsemblBacteria; AAM86731; AAM86731; y3181.
DR EnsemblBacteria; AAS63046; AAS63046; YP_2864.
DR GeneID; 57973842; -.
DR KEGG; ype:YPO0793; -.
DR KEGG; ypk:y3181; -.
DR KEGG; ypm:YP_2864; -.
DR PATRIC; fig|214092.21.peg.1055; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_8_6; -.
DR OMA; ANWVYLE; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR HAMAP; MF_01162; Aas; 1.
DR InterPro; IPR023775; Aas.
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.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SMART; SM00563; PlsC; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Acyltransferase; ATP-binding; Cell inner membrane; Cell membrane; Ligase;
KW Membrane; Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..718
FT /note="Bifunctional protein Aas"
FT /id="PRO_0000193055"
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
FT TRANSMEM 409..433
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
FT REGION 15..138
FT /note="Acyltransferase"
FT REGION 233..646
FT /note="AMP-binding"
FT ACT_SITE 36
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
FT CONFLICT 366
FT /note="G -> D (in Ref. 3; AAS63046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 79386 MW; C0AB5A05BBCB6C35 CRC64;
MAYRLLRALF RGLFRVTIDG VTDQFKHEKL IITPNHVSFL DGALLALFLP IKPVFAVYTS
ITDTWYMRWL KPYVDFVALD PTNPMAIKHL VRMVEQGRPV VIFPEGRITV TGSLMKIYDG
AAFVAAKSGA AVVPIRLDGP EFTHFGRLQG VLKTRWFPKI SIHVLPATTI PMPQAPRSRE
RRVLAGEHLH TIMMAARMAT VPRETLFEAL LSAQTRYGRF KPCIEDVSFK EDSYQTLLKK
TLGVSRILQR FTVPGEHVGM LLPNATITAA AIFGASLRGR IPALLNYTSG AKGLQSAIIA
ASLKTIVTSR QFLEKGKLTH LPEQVNEVNW VYLEDLKDTV TLTDKLWILF HLCFPRRAML
PQQADGSALI LFTSGSEGNP KGVVHSHASL LANVEQIRTI ADFTPRDRFM SSLPLFHAFG
LTVGLFTPLM TGSRVFLYPS PLHYRVVPEL VYDRNCTVLF GTSTFLGNYA RFAHPYDFAR
VRYVVAGAEK LAESTKQIWQ DKFGIRILEG YGVTECAPVV AINVPMAAKV NTVGRILPGM
EARLINVPGI AQGGRLQLRG PNIMRGYLRV ENPGVLEQPS AENAQGELDA NWYDTGDIVT
LDEQGFCAIR GRVKRFAKLA GEMVSLESVE QLAISLSPEG QHAAAAKTDS AKGEALVLFT
TDSEITRERL IKVARENGVP ELAVPRDIRV VKALPLLGSG KPDFVTLGKM AQDPEMSV
