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   27-MAR-2024, entry version 107.
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};
GN   OrderedLocusNames=NMB0413;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Pseudomonadota; 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; 122586-NMB0413; -.
DR   DNASU; 902529; -.
DR   GeneID; 61281983; -.
DR   KEGG; nme:NMB0413; -.
DR   PATRIC; fig|122586.8.peg.523; -.
DR   HOGENOM; CLU_009289_6_2_4; -.
DR   InParanoid; P0A0U9; -.
DR   OrthoDB; 9789078at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000425; Chromosome.
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; 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; 1.10.150.770; -; 1.
DR   Gene3D; 3.30.450.330; -; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 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   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 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
//