ID   PBP2_NEIFL              Reviewed;         400 AA.
AC   P16873;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Probable peptidoglycan D,D-transpeptidase PenA {ECO:0000305};
DE            EC=3.4.16.4 {ECO:0000250|UniProtKB:P0AD68};
DE   AltName: Full=Penicillin-binding protein 2 {ECO:0000303|PubMed:2510173};
DE            Short=PBP-2 {ECO:0000303|PubMed:2510173};
DE   Flags: Fragment;
GN   Name=penA {ECO:0000303|PubMed:2510173};
OS   Neisseria flavescens.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2510173; DOI=10.1073/pnas.86.22.8988;
RA   Spratt B.G., Zhang Q.-Y., Jones D.M., Hutchison A., Brannigan J.A.,
RA   Dowson C.G.;
RT   "Recruitment of a penicillin-binding protein gene from Neisseria flavescens
RT   during the emergence of penicillin resistance in Neisseria meningitidis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:8988-8992(1989).
CC   -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC       division septum. {ECO:0000250|UniProtKB:P0AD68}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P0AD68};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000250|UniProtKB:P0AD68}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AD68}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P0AD68}.
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:0000305}.
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DR   EMBL; M26645; AAA25464.1; -; Genomic_DNA.
DR   PIR; B36190; B36190.
DR   AlphaFoldDB; P16873; -.
DR   SMR; P16873; -.
DR   STRING; 596320.NEIFL0001_0100; -.
DR   MEROPS; X52.001; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF00905; Transpeptidase; 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; Septation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..400
FT                   /note="Probable peptidoglycan D,D-transpeptidase PenA"
FT                   /id="PRO_0000195450"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD68"
FT   NON_TER         1
SQ   SEQUENCE   400 AA;  42861 MW;  AAC81B8778CEB93C CRC64;
     NIDGKGQEGL ELSREDSLRG EDGAKVVLRD NKGNIVDSLD SPRNSVPKNG QDMILSLDQR
     IQTLAYDELN KAVAYHKAKA GAVVVLDAQT GEILALVNSP AYDPNQPGQA NSEQRRNRAV
     TDMIEPGSAM KPFTIAKALD SGKVDPTDTF NTLPYKIGPA TVQDTHVYPT LDVRGIMQKS
     SNVGTSKLSA MFTPKEMYDF YHDLGVGVRM HSGFPGETAG LLRSWRRWQK IEQATMSFGY
     GLQLSLLQLA RAYTVLTHDG ELLPVSFEKQ AVAPKGKRVI KASTAKKVRE LMVSVTEAGG
     TGIAGAVDGF DVGAKTGTAR KLVNGRYVDN KHVGTFIGFA PAKNPRVIVA VTIDEPTANG
     YYGGVVAGPV FKEVMSGSLN ILGVSPTKPL SNTATVKVPS