Reviewed, UniProtKB/Swiss-Prot A6TDH2 (AAS_KLEP7)

Names and origin

Protein names

Recommended name:
    Bifunctional protein aas
Including the following 2 domains:
    1- Recommended name:
            2-acylglycerophosphoethanolamine acyltransferase
              EC=2.3.1.40
        Alternative name(s):
            Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase
            2-acyl-GPE acyltransferase
    2- Recommended name:
            Acyl-[acyl-carrier-protein] synthetase
              EC=6.2.1.20
        Alternative name(s):
            Long-chain-fatty-acid--[acyl-carrier-protein] ligase
            Acyl-ACP synthetase

Gene names

Name:	aas
Ordered Locus Names:	KPN78578_31820
ORF Names:	KPN_03245

Organism

Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) [Complete proteome] [HAMAP]

Taxonomic identifier

272620 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	719 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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
Ligand	ATP-binding Nucleotide-binding
Molecular function	Acyltransferase Ligase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	metabolic 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: HAMAP long-chain-fatty-acid-[acyl-carrier-protein] ligase activity Inferred from electronic annotation. Source: HAMAP
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_1000065641
Regions
	Transmembrane	258 – 277	20	Potential
	Transmembrane	409 – 433	25	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)
	A6TDH2-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: BCCFD54F94137FCB	FASTA	719	80,214
	10 20 30 40 50 60 MLLGFFRLLF KGLYRVRLTG DTQALYQQKV LITPNHVSFL DGILLALFLP VRPVFAVYTS 70 80 90 100 110 120 ISQRWFMRAL TPIIDFVPLD PTKPMSIKHL VRLIEQGRPV VIFPEGRISV SGSLMKIYDG 130 140 150 160 170 180 AAFVAAKSQA TIVPLRIEGA ELTPFSRLKG LVKRRLFPRI QLHLLPPTHL PMPEAPRARD 190 200 210 220 230 240 RRKIAGEMLH QIMMEARMAV RPRETLYESL LAAQDRFGAR KPCVEDINFQ PDTYRKLLTK 250 260 270 280 290 300 TLFVARILEK YSQPGEKIGL MLPNAGISAA VIFGAIARGR IPAMMNYTAG VKGLSSAIAA 310 320 330 340 350 360 AELNTIFTSR TFLDKGKLWH LPEQLTQVRW VFLEDLKGDI TLADKLWIFA HLLAPRLAQV 370 380 390 400 410 420 KQQPEDAAMI LFTSGSEGNP KGVVHSHKSL LSNVEQIKTI ADFTANDRFM SALPLFHSFG 430 440 450 460 470 480 LTVGLLTPLL TGAEVFLYPS PLHYRVVPEL VYDRNCTVLF GTSTFLANYA RFANPYDFYR 490 500 510 520 530 540 LRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKV GTVGRILPGM 550 560 570 580 590 600 DARLLAMPGI DQGGRLQLKG PNIMKGYLRV ENPGVLEAPA AENQHGEMEA GWYDTGDIVT 610 620 630 640 650 660 FDEQGYVRIQ GRAKRFAKIA GEMISLEMVE QVALGASPDK MHATAIKQDA SKGEALVLFT 670 680 690 700 710 TDNELTREAL LRYARQHGVP ELAVPRDIRW LKQLPVLGSG KPDYVTLKNM VDEAETTHE

References

[1]	McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000647 Genomic DNA. Translation: ABR78643.1.
RefSeq	YP_001336873.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5341162.
GenomeReviews	Gene locus KPN78578_31820 in contig CP000647_GR.
KEGG	kpn:KPN_03245.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A6TDH2. KGYLRVE.
Family and domain databases
HAMAP	MF_01162. [Tree]
InterPro	IPR002123. Acyltransferase. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
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_KLEP7

Accession

Primary (citable) accession number: A6TDH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	August 21, 2007
Last modified:	June 16, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)