GenomeNet

Database: UniProt
Entry: Q51098_NEIME
LinkDB: Q51098_NEIME
Original site: Q51098_NEIME 
ID   Q51098_NEIME            Unreviewed;       582 AA.
AC   Q51098;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Probable peptidoglycan D,D-transpeptidase PenA {ECO:0000256|HAMAP-Rule:MF_02080};
DE            EC=3.4.16.4 {ECO:0000256|HAMAP-Rule:MF_02080};
DE   AltName: Full=Penicillin-binding protein 2 {ECO:0000256|HAMAP-Rule:MF_02080};
DE            Short=PBP-2 {ECO:0000256|HAMAP-Rule:MF_02080};
GN   Name=penA {ECO:0000256|HAMAP-Rule:MF_02080,
GN   ECO:0000313|EMBL:CAA42189.1};
OS   Neisseria meningitidis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=487 {ECO:0000313|EMBL:CAA42189.1};
RN   [1] {ECO:0000313|EMBL:CAA42189.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NM1072 {ECO:0000313|EMBL:CAA42189.1};
RA   Spratt B.G., Bowler L.D., Zhang Q.Y., Zhou J., Maynard-Smith J.;
RT   "The role of interspecies horizontal gene transfer in the evolution of
RT   penicillin resistance in pathogenic and commensal Neisseria species.";
RL   Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAP46602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M00.242888 {ECO:0000313|EMBL:AAP46603.1}, and M98.250718
RC   {ECO:0000313|EMBL:AAP46602.1};
RA   Sadler F.A., Borrow R., Ramsay M., Dawson M.M., Gray S.J., Kaczmarski E.B.,
RA   Fox A.J.;
RT   "Sequence analysis of the genetic diversity of the meningococcal penA
RT   gene.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AAM97217.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M4219 {ECO:0000313|EMBL:AAM97224.1}, M7723
RC   {ECO:0000313|EMBL:AAM97217.1}, M7725 {ECO:0000313|EMBL:AAM97222.1},
RC   M7731 {ECO:0000313|EMBL:AAM97221.1}, M7743
RC   {ECO:0000313|EMBL:AAM97218.1}, M7922 {ECO:0000313|EMBL:AAM97220.1},
RC   M7923 {ECO:0000313|EMBL:AAM97219.1}, and M7930
RC   {ECO:0000313|EMBL:AAM97223.1};
RA   Arreaza L., Sacchi C.T., Mayer L.W.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC       division septum. {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_02080};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02080}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02080}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02080}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02080}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY127636; AAM97217.1; -; Genomic_DNA.
DR   EMBL; AY127637; AAM97218.1; -; Genomic_DNA.
DR   EMBL; AY127638; AAM97219.1; -; Genomic_DNA.
DR   EMBL; AY127639; AAM97220.1; -; Genomic_DNA.
DR   EMBL; AY127640; AAM97221.1; -; Genomic_DNA.
DR   EMBL; AY127641; AAM97222.1; -; Genomic_DNA.
DR   EMBL; AY127642; AAM97223.1; -; Genomic_DNA.
DR   EMBL; AY127643; AAM97224.1; -; Genomic_DNA.
DR   EMBL; AF515085; AAP46602.1; -; Genomic_DNA.
DR   EMBL; AF515086; AAP46603.1; -; Genomic_DNA.
DR   EMBL; X59630; CAA42189.1; -; Genomic_DNA.
DR   PIR; S49092; S49092.
DR   RefSeq; WP_041421792.1; NZ_WIUG01000010.1.
DR   AlphaFoldDB; Q51098; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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; IEA:UniProtKB-KW.
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   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 {ECO:0000256|ARBA:ARBA00023251};
KW   Carboxypeptidase {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW   Rule:MF_02080};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02080}; Cell shape {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02080};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_02080};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_02080}.
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT   DOMAIN          71..220
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          263..557
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        310
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ   SEQUENCE   582 AA;  63756 MW;  59FB87C2D56E4E77 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 ARKLVNGRYV DYKHVATFIG FAPAKNPRVI VAVTIDEPTA
     NGYYGGVVTG PVFKQVMGGS LNILGVSPTK PLTNVAAVKT PS
//
DBGET integrated database retrieval system