ID PBP2_NEIGO Reviewed; 581 AA. AC P08149; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 04-NOV-2026, entry version 134. DE RecName: Full=Probable peptidoglycan D,D-transpeptidase PenA {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000305}; 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, ECO:0000303|PubMed:3126399}; DE Short=PBP-2 {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000303|PubMed:3126399}; GN Name=penA {ECO:0000255|HAMAP-Rule:MF_02080, GN ECO:0000303|PubMed:3126399}; OS Neisseria gonorrhoeae. OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=485; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3126399; DOI=10.1038/332173a0; RA Spratt B.G.; RT "Hybrid penicillin-binding proteins in penicillin-resistant strains of RT Neisseria gonorrhoeae."; RL Nature 332:173-176(1988). 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 -!- MISCELLANEOUS: This protein was sequenced in penicillin-sensitive CC strains LM306, and FA19, and in penicillin-resistant strains CDC84- CC 060384, CDC84-060418 and CDC77-124615. The sequence shown is that of CC strain LM306. CC -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily. CC {ECO:0000255|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; M32091; AAA25463.1; -; Genomic_DNA. DR EMBL; X07468; CAA30356.1; -; Genomic_DNA. DR EMBL; X07469; CAA30357.1; -; Genomic_DNA. DR EMBL; X07470; CAA30358.1; -; Genomic_DNA. DR PIR; S00916; S00916. DR RefSeq; WP_003695531.1; NZ_UGRJ01000003.1. DR RefSeq; WP_003703066.1; NZ_CP020415.2. DR RefSeq; WP_010360711.1; NZ_VCDA01000017.1. DR RefSeq; WP_047917829.1; NZ_SURE01000013.1. DR PDB; 3EQU; X-ray; 2.40 A; A/B=44-581. DR PDB; 3EQV; X-ray; 2.40 A; A/B=44-581. DR PDB; 4U3T; X-ray; 2.20 A; A/B=237-574. DR PDB; 5KSH; X-ray; 2.40 A; A/B=44-581. DR PDB; 6HZJ; X-ray; 1.43 A; A/B=238-581. DR PDB; 6P52; X-ray; 1.83 A; A/B=237-574. DR PDB; 6P53; X-ray; 1.92 A; A/B=237-574. DR PDB; 6P54; X-ray; 1.83 A; A/B=237-574. DR PDB; 6P55; X-ray; 1.74 A; A/B=237-574. DR PDB; 6P56; X-ray; 1.92 A; A/B=237-574. DR PDB; 6VBM; X-ray; 1.71 A; A/B=237-574. DR PDB; 6XQV; X-ray; 2.05 A; A/B=237-282, A/B=298-574. DR PDB; 6XQX; X-ray; 2.15 A; A/B=237-282, A/B=298-574. DR PDB; 6XQY; X-ray; 1.90 A; A/B=237-282, A/B=298-574. DR PDB; 6XQZ; X-ray; 2.04 A; A/B=237-282, A/B=298-574. DR PDB; 9OTG; X-ray; 3.15 A; A/B=237-574. DR AlphaFoldDB; P08149; -. DR SMR; P08149; -. DR IntAct; P08149; 1. DR DrugBank; DB00535; Cefdinir. DR MEROPS; X52.001; -. DR OMA; AADQYSD; -. DR BRENDA; 2.4.99.28; 3590. DR UniPathway; UPA00219; -. DR EvolutionaryTrace; P08149; -. 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:TreeGrafter. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. 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; IPR050515; Beta-lactam/transpept. 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 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Carboxypeptidase; Cell cycle; KW Cell division; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Hydrolase; Membrane; KW Peptidoglycan synthesis; Protease; Septation; Transmembrane; KW Transmembrane helix. FT CHAIN 1..581 FT /note="Probable peptidoglycan D,D-transpeptidase PenA" FT /id="PRO_0000195449" 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" FT VARIANT 346 FT /note="D -> DD (in strain: CDC84-060418, CDC77-124615 and FT CDC84-060384)" FT VARIANT 504 FT /note="F -> L (in strain: CDC84-060418, CDC77-124615 and FT CDC84-060384)" FT VARIANT 510 FT /note="A -> V (in strain: CDC84-060418, CDC77-124615 and FT CDC84-060384)" FT VARIANT 516 FT /note="A -> G (in strain: CDC84-060418, CDC77-124615 and FT CDC84-060384)" FT VARIANT 541 FT /note="H -> N (in strain: FA19 and CDC84-060418)" FT VARIANT 551 FT /note="P -> L (in strain: CDC84-060384)" FT VARIANT 551 FT /note="P -> S (in strain: CDC77-124615)" FT VARIANT 552 FT /note="P -> V (in strain: CDC84-060418)" FT VARIANT 555..556 FT /note="KI -> QV (in strain: CDC84-060418)" FT VARIANT 566 FT /note="I -> V (in strain: CDC84-060418)" FT VARIANT 574 FT /note="A -> NV (in strain: CDC84-060418)" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:3EQV" FT STRAND 65..71 FT /evidence="ECO:0007829|PDB:3EQU" FT HELIX 72..77 FT /evidence="ECO:0007829|PDB:3EQU" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:3EQU" FT STRAND 165..168 FT /evidence="ECO:0007829|PDB:3EQU" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:3EQU" FT HELIX 176..179 FT /evidence="ECO:0007829|PDB:3EQU" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:3EQU" FT HELIX 191..195 FT /evidence="ECO:0007829|PDB:3EQU" FT HELIX 197..201 FT /evidence="ECO:0007829|PDB:3EQU" FT STRAND 205..211 FT /evidence="ECO:0007829|PDB:3EQU" FT STRAND 217..220 FT /evidence="ECO:0007829|PDB:3EQU" FT HELIX 231..234 FT /evidence="ECO:0007829|PDB:3EQU" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:3EQU" FT HELIX 241..257 FT /evidence="ECO:0007829|PDB:6HZJ" FT STRAND 261..269 FT /evidence="ECO:0007829|PDB:6HZJ" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:6HZJ" FT STRAND 274..280 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:3EQU" FT HELIX 294..297 FT /evidence="ECO:0007829|PDB:3EQU" FT HELIX 300..303 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 313..322 FT /evidence="ECO:0007829|PDB:6HZJ" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:6HZJ" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:6HZJ" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:6HZJ" FT STRAND 351..354 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 355..360 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 364..371 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 376..385 FT /evidence="ECO:0007829|PDB:6HZJ" FT TURN 386..389 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 407..409 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 412..419 FT /evidence="ECO:0007829|PDB:6HZJ" FT STRAND 425..427 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 428..439 FT /evidence="ECO:0007829|PDB:6HZJ" FT TURN 440..442 FT /evidence="ECO:0007829|PDB:6HZJ" FT STRAND 448..450 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 464..474 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 475..477 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 485..487 FT /evidence="ECO:0007829|PDB:6HZJ" FT STRAND 495..526 FT /evidence="ECO:0007829|PDB:6HZJ" FT STRAND 529..537 FT /evidence="ECO:0007829|PDB:6HZJ" FT HELIX 545..563 FT /evidence="ECO:0007829|PDB:6HZJ" SQ SEQUENCE 581 AA; 63650 MW; A495A788E465EFA2 CRC64; MLIKSEYKPR MLPKEEQVKK PMTSNGRISF VLMAMAVLFA CLIARGLYLQ TVTYNFLKEQ GDNRIVRTQA LPATRGTVSD RNGAVLALSA PTESLFAVPK DMKEMPSAAQ LERLSELVDV PVDVLRNKLE QKGKSFIWIK RQLDPKVAEE VKALGLENFV FEKELKRHYP MGNLFAHVIG FTDIDGKGQE GLELSLEDSL YGEDGAEVVL RDRQGNIVDS LDSPRNKAPQ NGKDIILSLD QRIQTLAYEE LNKAVEYHQA KAGTVVVLDA RTGEILALAN TPAYDPNRPG RADSEQRRNR AVTDMIEPGS AIKPFVIAKA LDAGKTDLNE RLNTQPYKIG PSPVRDTHVY PSLDVRGIMQ KSSNVGTSKL SARFGAEEMY DFYHELGIGV RMHSGFPGET AGLLRNWRRW RPIEQATMSF GYGLQLSLLQ LARAYTALTH DGVLLPLSFE KQAVAPQGKR IFKESTAREV RNLMVSVTEP GGTGTAGAVD GFDVGAKTGT ARKFVNGRYA DNKHVATFIG FAPAKNPRVI VAVTIDEPTA HGYYGGVVAG PPFKKIMGGS LNILGISPTK PLTAAAVKTP S //