ID   AAS_SHIF8               Reviewed;         719 AA.
AC   Q0T128;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=SFV_2914;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA   Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA   Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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 (By
CC       similarity).
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 (By similarity).
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; CP000266; ABF04987.1; -; Genomic_DNA.
DR   RefSeq; YP_690292.1; -.
DR   GeneID; 4207218; -.
DR   GenomeReviews; CP000266_GR; SFV_2914.
DR   KEGG; sfv:SFV_2914; -.
DR   HOGENOM; Q0T128; -.
DR   OMA; Q0T128; KGYLRVE.
DR   BioCyc; SFLE373384:SFV_2914-MON; -.
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   3: Inferred from homology;
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_1000065643.
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       By similarity.
SQ   SEQUENCE   719 AA;  80668 MW;  BEFABABB23959F38 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 IPAMMNYTAG VKGLTSAITA
     AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TTADKVWIFA HLLMPRLAQV
     KQQPEEEALI LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTTNDRFM SALPLFHSFG
     LTVGLFTPLL TGAEVFLYPS PLHYRIVPDL 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
//