PBPA_NEIMB
ID PBPA_NEIMB Reviewed; 798 AA.
AC P0A0Z6; O05194;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Penicillin-binding protein 1A;
DE Short=PBP-1a;
DE Short=PBP1a;
DE Includes:
DE RecName: Full=Penicillin-insensitive transglycosylase;
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
DE AltName: Full=Peptidoglycan TGase;
DE Includes:
DE RecName: Full=Penicillin-sensitive transpeptidase;
DE EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
DE AltName: Full=DD-transpeptidase;
GN Name=mrcA; Synonyms=ponA; OrderedLocusNames=NMB1807;
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).
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000250|UniProtKB:P02918};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000250|UniProtKB:P02918};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000305}.
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DR EMBL; AE002098; AAF42144.1; -; Genomic_DNA.
DR PIR; H81040; H81040.
DR RefSeq; NP_274804.1; NC_003112.2.
DR RefSeq; WP_002219786.1; NC_003112.2.
DR AlphaFoldDB; P0A0Z6; -.
DR SMR; P0A0Z6; -.
DR STRING; 122586.NMB1807; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PaxDb; P0A0Z6; -.
DR EnsemblBacteria; AAF42144; AAF42144; NMB1807.
DR GeneID; 61280700; -.
DR KEGG; nme:NMB1807; -.
DR PATRIC; fig|122586.8.peg.2297; -.
DR HOGENOM; CLU_006354_2_4_4; -.
DR OMA; LAQMAMI; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR031376; PCB_OB.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF17092; PCB_OB; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Carboxypeptidase; Cell inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
KW Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..798
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000083172"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..798
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 50..218
FT /note="Transglycosylase"
FT REGION 378..700
FT /note="Transpeptidase"
FT REGION 738..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 461
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 798 AA; 88148 MW; 0B4F4EF037A9977B CRC64;
MIKKILTTCF GLVFGFCVFG VGLVAIAILV TYPKLPSLDS LQHYQPKMPL TIYSADGEVI
GMYGEQRREF TKIGDFPEVL RNAVIAAEDK RFYRHWGVDV WGVARAAVGN VVSGSVQSGA
STITQQVAKN FYLSSEKTFT RKFNEVLLAY KIEQSLSKDK ILELYFNQIY LGQRAYGFAS
AAQIYFNKNV RDLTLAEAAM LAGLPKAPSA YNPIVNPERA KLRQKYILNN MLEEKMITVQ
QRDQALNEEL HYERFVRKID QSALYVAEMV RQELYEKYGE DAYTQGFKVY TTVRADHQKV
ATEALRKALR NFDRGSSYRG AENYIDLSKS EDVEETVSQY LSGLYTVDKM VPAVVLDVTK
KKNVVIQLPG GRRVTLDRRA LGFAARAVNN EKMGEDRIRR GAVIRVKNNG GRWAVVQEPL
LQGALVSLDA KTGAVRALVG GYDFHSKTFN RAVQAMRQPG STFKPFVYSA ALSKGMTAST
VVNDAPISLP GKGPNGSVWT PKNSDGRYSG YITLRQALTA SKNMVSIRIL MSIGVGYAQQ
YIRRFGFRSS ELPASLSMAL GTGETTPLKV AEAYSVFANG GYRVSSHVID KIYDRDGRLR
AQMQPLVAGQ NAPQAIDPRN AYIMYKIMQD VVRVGTARGA AALGRTDIAG KTGTTNDNKD
AWFVGFNPDV VTAVYIGFDK PKSMGRVGYG GTIAVPVWVD YMRFALKGKQ GKGMKMPEGV
VSSNGEYYMK ERMVTDPGLT LDNSGIAPQP SRRAKEDDGG AAEGGRQAAD DEVRQDMQET
PVLPSNTGSK QQQLDSLF
