PBP2_NEIMB
ID PBP2_NEIMB Reviewed; 581 AA.
AC P0A0U9; P11882;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable peptidoglycan D,D-transpeptidase PenA {ECO:0000255|HAMAP-Rule:MF_02080};
DE EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02080};
DE AltName: Full=Penicillin-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_02080};
DE Short=PBP-2 {ECO:0000255|HAMAP-Rule:MF_02080};
GN Name=penA {ECO:0000255|HAMAP-Rule:MF_02080}; OrderedLocusNames=NMB0413;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C311 / Serogroup B;
RX PubMed=2503813; DOI=10.1093/nar/17.13.5383;
RA Xhang Q.-Y., Spratt B.G.;
RT "Nucleotide sequence of the penicillin-binding protein 2 gene of Neisseria
RT meningitidis.";
RL Nucleic Acids Res. 17:5383-5383(1989).
RN [2]
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: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC division septum. {ECO:0000255|HAMAP-Rule:MF_02080}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02080};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02080}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02080}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02080}.
CC -!- DOMAIN: The enzyme has an N-terminal penicillin insensitive
CC transglycosylase domain (formation of linear glycan strands) and a C-
CC terminal penicillin-sensitive transpeptidase domain (cross-linking of
CC the peptide subunits).
CC -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02080}.
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DR EMBL; X15276; CAA33347.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF40852.1; -; Genomic_DNA.
DR PIR; S04857; S04857.
DR RefSeq; NP_273462.1; NC_003112.2.
DR RefSeq; WP_002218783.1; NC_003112.2.
DR AlphaFoldDB; P0A0U9; -.
DR SMR; P0A0U9; -.
DR STRING; 122586.NMB0413; -.
DR MEROPS; X52.001; -.
DR PaxDb; P0A0U9; -.
DR DNASU; 902529; -.
DR EnsemblBacteria; AAF40852; AAF40852; NMB0413.
DR GeneID; 61281983; -.
DR KEGG; nme:NMB0413; -.
DR PATRIC; fig|122586.8.peg.523; -.
DR HOGENOM; CLU_009289_6_2_4; -.
DR OMA; HGKEEYY; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR HAMAP; MF_02080; FtsI_transpept; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR037532; FtsI_transpept.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56519; SSF56519; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Carboxypeptidase; Cell cycle; Cell division;
KW Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Peptidoglycan synthesis; Protease; Reference proteome; Septation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..581
FT /note="Probable peptidoglycan D,D-transpeptidase PenA"
FT /id="PRO_0000195452"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT ACT_SITE 310
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
SQ SEQUENCE 581 AA; 63604 MW; BABC396F205D2F6B CRC64;
MLIKSEYKPR MLPKEEQVKK PMTSNGRISF VLMAIAVLFA GLIARGLYLQ TVTYNFLKEQ
GDNRIVRTQT LPATRGTVSD RNGAVLALSA PTESLFAVPK EMKEMPSAAQ LERLSELVDV
PVDVLRNKLE QKGKSFIWIK RQLDPKVAEE VKALGLENFV FEKELKRHYP MGNLFAHVIG
FTDIDGKGQE GLELSLEDSL HGEDGAEVVL RDRQGNIVDS LDSPRNKAPK NGKDIILSLD
QRIQTLAYEE LNKAVEYHQA KAGTVVVLDA RTGEILALAN TPAYDPNRPG RADSEQRRNR
AVTDMIEPGS AIKPFVIAKA LDAGKTDLNE RLNTQPYKIG PSPVRDTHVY PSLDVRGIMQ
KSSNVGTSKL SARFGAEEMY DFYHELGIGV RMHSGFPGET AGLLRNWRRW RPIEQATMSF
GYGLQLSLLQ LARAYTALTH DGVLLPVSFE KQAVAPQGKR IFKESTAREV RNLMVSVTEP
GGTGTAGAVD GFDVGAKTGT ARKFVNGRYA DNKHIATFIG FAPAKNPRVI VAVTIDEPTA
HGYYGGVVAG PPFKKIMGGS LNILGISPTK PLTAAAVKTP S
