Q74RZ6 (AAS_YERPE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein aas

Including the following 2 domains:

1. 2-acylglycerophosphoethanolamine acyltransferase
   EC=2.3.1.40
   Alternative name(s):
   2-acyl-GPE acyltransferase
   Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase
2. Acyl-[acyl-carrier-protein] synthetase
   EC=6.2.1.20
   Alternative name(s):
   Acyl-ACP synthetase
   Long-chain-fatty-acid--[acyl-carrier-protein] ligase

Gene names

Name:	aas
Ordered Locus Names:	YPO0793, y3181, YP_2864

Organism

Yersinia pestis

Taxonomic identifier

632 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	718 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1 By similarity. HAMAP MF_01162
Catalytic activity	Acyl-[acyl-carrier-protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = [acyl-carrier-protein] + O-(1-beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine. HAMAP MF_01162 ATP + an acid + [acyl-carrier-protein] = AMP + diphosphate + acyl-[acyl-carrier-protein]. HAMAP MF_01162
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_01162.
Sequence similarities	In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Sequence caution	The sequence AAM86731.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Acyltransferase Ligase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: InterPro phospholipid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity Inferred from electronic annotation. Source: EC long-chain fatty acid [acyl-carrier-protein] ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 718	718	Bifunctional protein aas HAMAP MF_01162		PRO_0000193055
Regions
	Transmembrane	258 – 277	20	Helical; Potential
	Transmembrane	409 – 433	25	Helical; Potential
	Region	15 – 138	124	Acyltransferase HAMAP MF_01162
	Region	233 – 646	414	AMP-binding HAMAP MF_01162
Sites
	Active site	36	1	By similarity
Experimental info
	Sequence conflict	366	1	G → D in AAS63046. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q74RZ6 [UniParc]. Last modified April 26, 2005. Version 2. Checksum: C0AB5A05BBCB6C35	FASTA	718	79,386
	10 20 30 40 50 60 MAYRLLRALF RGLFRVTIDG VTDQFKHEKL IITPNHVSFL DGALLALFLP IKPVFAVYTS 70 80 90 100 110 120 ITDTWYMRWL KPYVDFVALD PTNPMAIKHL VRMVEQGRPV VIFPEGRITV TGSLMKIYDG 130 140 150 160 170 180 AAFVAAKSGA AVVPIRLDGP EFTHFGRLQG VLKTRWFPKI SIHVLPATTI PMPQAPRSRE 190 200 210 220 230 240 RRVLAGEHLH TIMMAARMAT VPRETLFEAL LSAQTRYGRF KPCIEDVSFK EDSYQTLLKK 250 260 270 280 290 300 TLGVSRILQR FTVPGEHVGM LLPNATITAA AIFGASLRGR IPALLNYTSG AKGLQSAIIA 310 320 330 340 350 360 ASLKTIVTSR QFLEKGKLTH LPEQVNEVNW VYLEDLKDTV TLTDKLWILF HLCFPRRAML 370 380 390 400 410 420 PQQADGSALI LFTSGSEGNP KGVVHSHASL LANVEQIRTI ADFTPRDRFM SSLPLFHAFG 430 440 450 460 470 480 LTVGLFTPLM TGSRVFLYPS PLHYRVVPEL VYDRNCTVLF GTSTFLGNYA RFAHPYDFAR 490 500 510 520 530 540 VRYVVAGAEK LAESTKQIWQ DKFGIRILEG YGVTECAPVV AINVPMAAKV NTVGRILPGM 550 560 570 580 590 600 EARLINVPGI AQGGRLQLRG PNIMRGYLRV ENPGVLEQPS AENAQGELDA NWYDTGDIVT 610 620 630 640 650 660 LDEQGFCAIR GRVKRFAKLA GEMVSLESVE QLAISLSPEG QHAAAAKTDS AKGEALVLFT 670 680 690 700 710 TDSEITRERL IKVARENGVP ELAVPRDIRV VKALPLLGSG KPDFVTLGKM AQDPEMSV

References

[1]	"Genome sequence of Yersinia pestis, the causative agent of plague." Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:523-527(2001) [PubMed: 11586360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CO-92 / Biovar Orientalis.
[2]	"Genome sequence of Yersinia pestis KIM." Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. , Matson J.S., Blattner F.R., Perry R.D. J. Bacteriol. 184:4601-4611(2002) [PubMed: 12142430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KIM5 / Biovar Mediaevalis.
[3]	"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans." Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R. DNA Res. 11:179-197(2004) [PubMed: 15368893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL590842 Genomic DNA. Translation: CAL19465.1. AE009952 Genomic DNA. Translation: AAM86731.1. Different initiation. AE017042 Genomic DNA. Translation: AAS63046.1.
PIR	AG0097.
RefSeq	NP_994169.1. NC_005810.1. YP_002345848.1. NC_003143.1.
3D structure databases
ProteinModelPortal	Q74RZ6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q74RZ6. 2 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1173632. 2766888.
GenomeReviews	Gene locus y3181 in contig AE009952_GR. Gene locus YP_2864 in contig AE017042_GR. Gene locus YPO0793 in contig AL590842_GR.
KEGG	ype:YPO0793. ypk:y3181. ypm:YP_2864.
PATRIC	18590746. VBIYerPes7843_1110.
Phylogenomic databases
HOGENOM	HBG361068.
OMA	ANWVYLE.
ProtClustDB	PRK08043.
Enzyme and pathway databases
BioCyc	YPES187410:Y3181-MONOMER. YPES214092:YPO0793-MONOMER.
Family and domain databases
HAMAP	MF_01162. Aas. [Tree]
InterPro	IPR002123. Acyltransferase. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR023775. Bifunctional_Aas. [Graphical view]
KO	K05939.
Pfam	PF01553. Acyltransferase. 1 hit. PF00501. AMP-binding. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AAS_YERPE

Accession

Primary (citable) accession number: Q74RZ6
Secondary accession number(s): Q0WIP0, Q8CZY1, Q8ZHU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program