ID   AAS_ECOLI               Reviewed;         719 AA.
AC   P31119; Q2MA01; Q46935; Q6IU49;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   16-JUN-2009, entry version 79.
DE   RecName: Full=Bifunctional protein aas;
DE   Includes:
DE     RecName: Full=2-acylglycerophosphoethanolamine acyltransferase;
DE              EC=2.3.1.40;
DE     AltName: Full=Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase;
DE     AltName: Full=2-acyl-GPE acyltransferase;
DE   Includes:
DE     RecName: Full=Acyl-[acyl-carrier-protein] synthetase;
DE              EC=6.2.1.20;
DE     AltName: Full=Long-chain-fatty-acid--[acyl-carrier-protein] ligase;
DE     AltName: Full=Acyl-ACP synthetase;
GN   Name=aas; OrderedLocusNames=b2836, JW2804;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=94132066; PubMed=8300626;
RA   Jackowski S., Jackson P.D., Rock C.O.;
RT   "Sequence and function of the aas gene in Escherichia coli.";
RL   J. Biol. Chem. 269:2921-2928(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-311.
RC   STRAIN=B / Bc251;
RX   MEDLINE=22549866; PubMed=12664169; DOI=10.1007/s00239-002-2423-0;
RA   Lenski R.E., Winkworth C.L., Riley M.A.;
RT   "Rates of DNA sequence evolution in experimental populations of
RT   Escherichia coli during 20,000 generations.";
RL   J. Mol. Evol. 56:498-508(2003).
RN   [5]
RP   FUNCTION.
RC   STRAIN=K12;
RX   PubMed=1649829;
RA   Hsu L., Jackowski S., Rock C.O.;
RT   "Isolation and characterization of Escherichia coli K-12 mutants
RT   lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and
RT   acyl-acyl carrier protein synthetase activity.";
RL   J. Biol. Chem. 266:13783-13788(1991).
RN   [6]
RP   MUTAGENESIS OF HIS-36.
RC   STRAIN=K12;
RX   MEDLINE=98175664; PubMed=9515909;
RA   Heath R.J., Rock C.O.;
RT   "A conserved histidine is essential for glycerolipid acyltransferase
RT   catalysis.";
RL   J. Bacteriol. 180:1425-1430(1998).
CC   -!- FUNCTION: Plays a role in lysophospholipid acylation. Transfers
CC       fatty acids to the 1-position via an enzyme-bound acyl-ACP
CC       intermediate in the presence of ATP and magnesium. Its
CC       physiological function is to regenerate phosphatidylethanolamine
CC       from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by
CC       transacylation reactions or degradation by phospholipase A1.
CC   -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + O-(2-acyl-sn-
CC       glycero-3-phospho)ethanolamine = [acyl-carrier-protein] + O-(1-
CC       beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine.
CC   -!- CATALYTIC ACTIVITY: ATP + an acid + [acyl-carrier-protein] = AMP +
CC       diphosphate + acyl-[acyl-carrier-protein].
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE
CC       acetyltransferase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ATP-
CC       dependent AMP-binding enzyme family.
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DR   EMBL; L14681; AAA17550.1; -; Unassigned_DNA.
DR   EMBL; U29581; AAB40483.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75875.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76905.1; -; Genomic_DNA.
DR   EMBL; AY625100; AAT42454.1; -; Genomic_DNA.
DR   PIR; E65066; E65066.
DR   RefSeq; AP_003399.1; -.
DR   RefSeq; NP_417313.1; -.
DR   HSSP; P08659; 1LCI.
DR   DIP; DIP:9025N; -.
DR   GeneID; 947315; -.
DR   GenomeReviews; AP009048_GR; JW2804.
DR   GenomeReviews; U00096_GR; b2836.
DR   KEGG; ecj:JW2804; -.
DR   KEGG; eco:b2836; -.
DR   EchoBASE; EB1630; -.
DR   EcoGene; EG11679; aas.
DR   HOGENOM; P31119; -.
DR   OMA; P31119; KGYLRVE.
DR   BioCyc; EcoCyc:AAS-MON; -.
DR   BioCyc; MetaCyc:AAS-MON; -.
DR   BRENDA; 2.3.1.40; 246.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-...; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008922; F:long-chain-fatty-acid-[acyl-carrier-protein...; IEA:HAMAP.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   HAMAP; MF_01162; -; 1.
DR   InterPro; IPR002123; Acyltransferase.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SMART; SM00563; PlsC; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; ATP-binding; Cell inner membrane; Cell membrane;
KW   Complete proteome; Ligase; Membrane; Multifunctional enzyme;
KW   Nucleotide-binding; Transferase; Transmembrane.
FT   CHAIN         1    719       Bifunctional protein aas.
FT                                /FTId=PRO_0000193046.
FT   TRANSMEM    258    277       Potential.
FT   TRANSMEM    409    433       Potential.
FT   REGION       15    138       Acyltransferase.
FT   REGION      233    646       AMP-binding.
FT   ACT_SITE     36     36
FT   MUTAGEN      36     36       H->A: Loss of 2-acyl-GPE acyltransferase
FT                                activity; retains acyl-ACP synthetase
FT                                activity.
FT   CONFLICT     15     16       RV -> AL (in Ref. 1; AAA17550).
FT   CONFLICT    202    202       P -> S (in Ref. 1; AAA17550).
FT   CONFLICT    281    281       M -> I (in Ref. 4; AAT42454).
SQ   SEQUENCE   719 AA;  80700 MW;  F4F1021E57835EB2 CRC64;
     MLFSFFRNLC RVLYRVRVTG DTQALKGERV LITPNHVSFI DGILLGLFLP VRPVFAVYTS
     ISQQWYMRWL KSFIDFVPLD PTQPMAIKHL VRLVEQGRPV VIFPEGRITT TGSLMKIYDG
     AGFVAAKSGA TVIPVRIEGA ELTHFSRLKG LVKRRLFPQI TLHILPPTQV AMPDAPRARD
     RRKIAGEMLH QIMMEARMAV RPRETLYESL LSAMYRFGAG KKCVEDVNFT PDSYRKLLTK
     TLFVGRILEK YSVEGERIGL MLPNAGISAA VIFGAIARRR MPAMMNYTAG VKGLTSAITA
     AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TTADKVWIFA HLLMPRLAQV
     KQQPEEEALI LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTTNDRFM SALPLFHSFG
     LTVGLFTPLL TGAEVFLYPS PLHYRIVPEL VYDRSCTVLF GTSTFLGHYA RFANPYDFYR
     LRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPGM
     DARLLSVPGI EEGGRLQLKG PNIMNGYLRV EKPGVLEVPT AENVRGEMER GWYDTGDIVR
     FDEQGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSPDK VHATAIKSDA SKGEALVLFT
     TDNELTRDKL QQYAREHGVP ELAVPRDIRY LKQMPLLGSG KPDFVTLKSW VDEAEQHDE
//