PA1_NEIMB
ID PA1_NEIMB Reviewed; 382 AA.
AC Q9K0U7;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Putative phospholipase A1;
DE EC=3.1.1.32;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 1-acylhydrolase;
DE Flags: Precursor;
GN OrderedLocusNames=NMB0464;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=NZ98/254 / Serogroup B;
RX PubMed=16645985; DOI=10.1002/pmic.200500821;
RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT prepared from the group B strain NZ98/254.";
RL Proteomics 6:3400-3413(2006).
CC -!- FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC
CC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is
CC bound by different amino acids with binding of each Ca(2+) shared with
CC ligands coming from each monomer. The Ca(2+) ion may have a role in
CC catalysis. {ECO:0000250};
CC -!- SUBUNIT: Homodimer; dimerization is reversible, and the dimeric form is
CC the active one. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=One of the very few enzymes
CC located there. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC used as vaccines in human.
CC -!- SIMILARITY: Belongs to the phospholipase A1 family. {ECO:0000305}.
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DR EMBL; AE002098; AAF40901.1; -; Genomic_DNA.
DR PIR; E81195; E81195.
DR RefSeq; NP_273511.1; NC_003112.2.
DR RefSeq; WP_002216585.1; NC_003112.2.
DR AlphaFoldDB; Q9K0U7; -.
DR SMR; Q9K0U7; -.
DR STRING; 122586.NMB0464; -.
DR PaxDb; Q9K0U7; -.
DR EnsemblBacteria; AAF40901; AAF40901; NMB0464.
DR GeneID; 61281934; -.
DR KEGG; nme:NMB0464; -.
DR PATRIC; fig|122586.8.peg.608; -.
DR HOGENOM; CLU_045813_0_0_4; -.
DR OMA; GAEMNTR; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00541; OMPLA; 1.
DR Gene3D; 2.40.230.10; -; 1.
DR InterPro; IPR003187; PLipase_A1.
DR InterPro; IPR036541; PLipase_A1_sf.
DR PANTHER; PTHR40457; PTHR40457; 1.
DR Pfam; PF02253; PLA1; 1.
DR PRINTS; PR01486; PHPHLIPASEA1.
DR SUPFAM; SSF56931; SSF56931; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell outer membrane; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Reference proteome; Signal;
KW Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..382
FT /note="Putative phospholipase A1"
FT /id="PRO_0000349892"
FT TOPO_DOM 28..65
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..78
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..183
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..189
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..202
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..233
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..236
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..250
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..272
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..274
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..284
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..313
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..315
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..325
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..341
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..346
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..356
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..377
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..382
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 250
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in dimeric form"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in dimeric form"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="in monomeric form"
FT /evidence="ECO:0000250"
SQ SEQUENCE 382 AA; 42714 MW; B468A802F062E836 CRC64;
MPTMGAEMNT RNMRYILLTG LLPMASAFGE TALQCAALTD NVTRLACYDR IFAAQLPSSA
GQEGQESKAV LNLTETVRSS LDKGEAVIVV EKGGDALPAD SAGETADIYT PLSLMYDLDK
NDLRGLLGVR EHNPMYLMPL WYNNSPNYAP GSPTRGTTVQ EKFGQQKRAE TKLQVSFKSK
IAEDLFKTRA DLWFGYTQRS DWQIYNQGRK SAPFRNTDYK PEIFLTQPVK ADLPFGGRLR
MLGAGFVHQS NGQSRPESRS WNRIYAMAGM EWGKLTVIPR VWVRAFDQSG DKNDNPDIAD
YMGYGDVKLQ YRLNDRQNVY SVLRYNPKTG YGAIEAAYTF PIKGKLKGVV RGFHGYGESL
IDYNHKQNGI GIGLMFNDLD GI
