PBP2_NEIGO
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 03-AUG-2022, entry version 122.
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, ECO:0000303|PubMed:3126399};
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC 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}.
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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_UGRK01000002.1.
DR RefSeq; WP_010360711.1; NZ_VAHL01000014.1.
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 PDBsum; 3EQU; -.
DR PDBsum; 3EQV; -.
DR PDBsum; 4U3T; -.
DR PDBsum; 5KSH; -.
DR PDBsum; 6HZJ; -.
DR PDBsum; 6P52; -.
DR PDBsum; 6P53; -.
DR PDBsum; 6P54; -.
DR PDBsum; 6P55; -.
DR PDBsum; 6P56; -.
DR PDBsum; 6VBM; -.
DR PDBsum; 6XQV; -.
DR PDBsum; 6XQX; -.
DR PDBsum; 6XQY; -.
DR PDBsum; 6XQZ; -.
DR AlphaFoldDB; P08149; -.
DR SMR; P08149; -.
DR IntAct; P08149; 1.
DR MINT; P08149; -.
DR DrugBank; DB00535; Cefdinir.
DR MEROPS; X52.001; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P08149; -.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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 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 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 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 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
