ID A0A448VHD7_9NEIS Unreviewed; 687 AA.
AC A0A448VHD7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidoglycan D,D-transpeptidase MrdA {ECO:0000256|HAMAP-Rule:MF_02081};
DE EC=3.4.16.4 {ECO:0000256|HAMAP-Rule:MF_02081};
DE AltName: Full=Penicillin-binding protein 2 {ECO:0000256|HAMAP-Rule:MF_02081};
DE Short=PBP-2 {ECO:0000256|HAMAP-Rule:MF_02081};
GN Name=penA_1 {ECO:0000313|EMBL:VEJ49170.1};
GN Synonyms=mrdA {ECO:0000256|HAMAP-Rule:MF_02081};
GN ORFNames=NCTC12742_00063 {ECO:0000313|EMBL:VEJ49170.1};
OS Neisseria weaveri.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=28091 {ECO:0000313|EMBL:VEJ49170.1, ECO:0000313|Proteomes:UP000272771};
RN [1] {ECO:0000313|EMBL:VEJ49170.1, ECO:0000313|Proteomes:UP000272771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12742 {ECO:0000313|EMBL:VEJ49170.1,
RC ECO:0000313|Proteomes:UP000272771};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall.
CC {ECO:0000256|HAMAP-Rule:MF_02081}.
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_02081};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02081}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02081}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02081}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02081}.
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DR EMBL; LR134533; VEJ49170.1; -; Genomic_DNA.
DR RefSeq; WP_004284702.1; NZ_POXI01000005.1.
DR AlphaFoldDB; A0A448VHD7; -.
DR STRING; 28091.SAMEA3174300_00719; -.
DR KEGG; nwe:SAMEA3174300_0719; -.
DR OrthoDB; 9789078at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000272771; Chromosome 1.
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-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR HAMAP; MF_02081; MrdA_transpept; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR017790; Penicillin-binding_protein_2.
DR NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 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_02081};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02081}; Cell shape {ECO:0000256|HAMAP-Rule:MF_02081};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02081};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02081};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02081};
KW Protease {ECO:0000256|HAMAP-Rule:MF_02081};
KW Reference proteome {ECO:0000313|Proteomes:UP000272771};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 68..243
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 276..618
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 335
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 687 AA; 76684 MW; 0622640C6E74E2DA CRC64;
MKTPRQHTQT VKDEAALQKD FLLRLVVAFI FIIILFVVLL SRFVYLQIIK HEEFTTKAVN
NRVSLIPTPP TRGEIIDVNG VVLAHNYPAY SLEIIPNQLE GKVDEVIELL KQYVDITETD
LKRFKKFRAE FSSYEKIPLK LKLNADEAAQ LAAQLYRFKG VEINARTFRE YPYGELTAHF
LGYIGRISDR DQKKLNEDNL ASLYRGSTHI GKSGLESYYE SQLHGLPGYQ EVEKDAYGHV
VRVLKTVPAQ TGQTLRLAMD IRLQREADRL MSGRRGAMIA IDPQTGGVLA FVSKPTFDPN
LFIDGIDSET WKKLNDDWQR PLINRVTQGL YPPGSTFKPF MGMALLESGK INQSSIVPAP
GAWSIPGTRH LFRDSVRSGH GSANLSKAIQ VSSDTFFYRL GYELGIDKTA PYLAEFGLGE
PTGIDLPHEY RGVLPSKEWK AKRFAKSKNP SQRKWNPAEM VSVSIGQGYN TYTPLQMAHA
TASLANDGVV YRPHMVKELL DHERQQITVI EPKPTKLIPF KRSNFEYIKQ SMVKVLKPGG
TAWRVGSGLQ YTMGGKTGTA QVVQIKQGQT YNAAALAEQH RDHAWFISFA PLDSPQIAIA
VILENGGWGA NAAPLARSLS DFYLLKLRGG NAGFSEEDAK SVKTSPKKQD NLLLATSLPT
SKLNTSIYQK AYEAVNNASA SGIRTNE
//
