ID D3RHS3_KLEVT Unreviewed; 719 AA.
AC D3RHS3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 29-MAY-2013, entry version 24.
DE RecName: Full=Bifunctional protein aas;
GN Name=aas; OrderedLocusNames=Kvar_0825;
OS Klebsiella variicola (strain At-22).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Klebsiella.
OX NCBI_TaxID=640131;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-22;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Pinto A.,
RA Currie C., Woyke T.;
RT "Complete sequence of Klebsiella variicola At-22.";
RL Submitted (FEB-2010) 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 inner membrane; Multi-pass membrane
CC protein (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC protein (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.
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DR EMBL; CP001891; ADC56755.1; -; Genomic_DNA.
DR RefSeq; YP_003437767.1; NC_013850.1.
DR ProteinModelPortal; D3RHS3; -.
DR EnsemblBacteria; ADC56755; ADC56755; Kvar_0825.
DR GeneID; 8780951; -.
DR KEGG; kva:Kvar_0825; -.
DR PATRIC; 32221717; VBIKleVar54872_0833.
DR HOGENOM; HOG000004907; -.
DR KO; K05939; -.
DR OMA; ANWVYLE; -.
DR BioCyc; KVAR640131:GHXG-839-MONOMER; -.
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; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR023775; Bifunctional_Aas.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
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; 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; 80274 MW; A1ED3C0699D4B344 CRC64;
MLLGFFRLLF KGLYRVRLTG DTQALYQQKV LITPNHVSFL DGILLALFLP VRPVFAVYTS
ISQRWFMRAL TPIIDFVPLD PTKPMSIKHL VRLIEQGRPV VIFPEGRISV SGSLMKIYDG
AAFVAAKSQA TIVPLRIDGA ELTPFSRLKG LVKRRLFPRI QLHLLPPTHL PMPEAPRARD
RRKIAGEMLH QIMMEARMAV RPRETLYESL LAAQDRFGAR KPCVEDINFQ PDTYRKLLTK
TLFVARILEK YSQRGEKIGL MLPNAGISAA VIFGAIARGR IPAMMNYTAG VKGLSSAIAA
AEINTIFTSR TFLDKGKLWH LPEQLTQVRW VFLEDLKGDI TLADKLWIFG HLLAPRLAQV
KQQPEDAAMI LFTSGSEGNP KGVVHSHKSL LANVEQIKTI ADFTANDRFM SALPLFHSFG
LTVGLLTPLF TGAEVFLYPS PLHYRVVPEL VYDRNCTVLF GTSTFLANYA RFANPYDFYR
LRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKV GTVGRILPGM
DARLLAMPGI EQGGRLQLKG PNIMKGYLRV ENPGVLEAPA AENQHGEKEA GWYDTGDIVT
FDEQGYVRIQ GRAKRFAKIA GEMISLEMVE QVALGASPDK MHATAIKQDA SKGEALVLFT
TDNELTREAL LRYARQHGVP ELAVPRDIRW LKQLPVLGSG KPDYVTLKNM VDEAETTHE
//
