ID C1ND49_9ESCH Unreviewed; 719 AA. AC C1ND49; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 21-SEP-2011, entry version 18. DE RecName: Full=Bifunctional protein aas; GN Name=aas; ORFNames=ESCG_00221; OS Escherichia sp. 1_1_43. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=457400; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_43; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Escherichia sp. strain 1_1_43."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. 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: ATP + an acid + [acyl-carrier-protein] = AMP + CC diphosphate + acyl-[acyl-carrier-protein]. 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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein CC (By similarity). CC -!- SIMILARITY: In the C-terminal section; belongs to the ATP- CC dependent AMP-binding enzyme family. CC -!- SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE CC acetyltransferase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG665830; EEH71534.1; -; Genomic_DNA. DR ProteinModelPortal; C1ND49; -. DR SMR; C1ND49; 206-696. 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-acyltransferase activity; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:HAMAP. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro. DR HAMAP; MF_01162; Aas; 1; -. DR InterPro; IPR002123; Acyltransferase. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR InterPro; IPR023775; Bifunctional_Aas. 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 Ligase; Membrane; Multifunctional enzyme; Nucleotide-binding; KW Transferase; Transmembrane; Transmembrane helix. FT TRANSMEM 258 277 Helical; (By similarity). FT TRANSMEM 409 433 Helical; (By similarity). FT REGION 15 138 Acyltransferase (By similarity). FT REGION 233 646 AMP-binding (By similarity). FT ACT_SITE 36 36 By similarity. 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 //