Q8Z406 (AAS_SALTI) 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:	STY3153, t2919

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	719 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.

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
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 – 719	719	Bifunctional protein aas HAMAP MF_01162		PRO_0000193052
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

Sequences

	Sequence		Length	Mass (Da)
	Q8Z406 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 41206B032CBF97E3	FASTA	719	80,477
	10 20 30 40 50 60 MLFGFFRNLF RVLYRVRVTG DVRALQGNRV LIAPNHVSFI DGMLLALFLP VRPVFAVYTS 70 80 90 100 110 120 ISQQWYMRWL TPLIDFVPLD PTKPMSIKHL VRLVEQGRPV VIFPEGRISV TGSLMKIYDG 130 140 150 160 170 180 AGFVAAKSGA TVIPLRIDGA ELTPFSRLKG LVKRRLFPRI QLHILPPTQI PMPEAPRARD 190 200 210 220 230 240 RRKIAGEMLH QIMMEARMAV RPRETLYESL LAAQYRYGAG KNCIEDINFT PDTYRKLLTK 250 260 270 280 290 300 TLFVGRILEK YSVEGEKIGL MLPNAAISAA VIFGAVSRRR IPAMMNYTAG VKGLTSAITA 310 320 330 340 350 360 AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TPADKLWIFA HLLAPRLAQV 370 380 390 400 410 420 KQQPEDAAII LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTANDRFM SALPLFHSFG 430 440 450 460 470 480 LTVGLFTPLL TGAEVFLYPS PLHYRIVPEL VYDRNCTVLF GTSTFLGNYA RFANPYDFYR 490 500 510 520 530 540 LRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPGM 550 560 570 580 590 600 DARLLAVPGI ENGGRLQLKG PNIMNGYLRV EKPGVLEVPS AENARGETER GWYDTGDIVR 610 620 630 640 650 660 FDENGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSAEK MHATAIKSDA SKGEALVLFT 670 680 690 700 710 TDSELTREKL QHYAREHGIP ELAVPRDIRY LKQLPLLGSG KPDFVTLKSW VDAPEQHHE

References

[1]

"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18." Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:848-852(2001) [PubMed: 11677608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT18.

[2]

"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18." Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R. J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL627277 Genomic DNA. Translation: CAD02835.1. AE014613 Genomic DNA. Translation: AAO70473.1.
RefSeq	NP_457404.1. NC_003198.1. NP_806613.1. NC_004631.1.
3D structure databases
ProteinModelPortal	Q8Z406.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1068660. 1249445.
GenomeReviews	Gene locus t2919 in contig AE014613_GR. Gene locus STY3153 in contig AL513382_GR.
KEGG	stt:t2919. sty:STY3153.
PATRIC	18544360. VBISalEnt120419_3207.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG361068.
OMA	ANWVYLE.
ProtClustDB	PRK08043.
Enzyme and pathway databases
BioCyc	SENT209261:T2919-MONOMER. SENT220341:STY3153-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_SALTI

Accession

Primary (citable) accession number: Q8Z406
Secondary accession number(s): Q7C7F5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program