ID A0A2M6VJF0_9BURK Unreviewed; 668 AA.
AC A0A2M6VJF0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=mrdA {ECO:0000256|HAMAP-Rule:MF_02081};
GN ORFNames=B9Z41_08835 {ECO:0000313|EMBL:PIT78496.1};
OS Limnohabitans sp. JirII-31.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1977908 {ECO:0000313|EMBL:PIT78496.1, ECO:0000313|Proteomes:UP000228925};
RN [1] {ECO:0000313|EMBL:PIT78496.1, ECO:0000313|Proteomes:UP000228925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JirII-31 {ECO:0000313|EMBL:PIT78496.1,
RC ECO:0000313|Proteomes:UP000228925};
RA Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA Simek K., Ghai R.;
RT "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL Submitted (APR-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIT78496.1}.
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; NESA01000005; PIT78496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M6VJF0; -.
DR OrthoDB; 9789078at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000228925; Unassembled WGS sequence.
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 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 Carboxypeptidase {ECO:0000256|HAMAP-Rule:MF_02081};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW 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:UP000228925};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 61..236
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 269..608
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 328
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 668 AA; 74344 MW; 5590C201305976D5 CRC64;
MRVIRNIEGD LRRFRERMVV VTAAILVAFL VLVLRLFYLQ VIRYEDLNEQ AENNRTAIVP
IVPNRGVIMD RNGIVLATNY SAYTLEITPS KLVVPLEEVI EQLASVVDIQ SRDKRRFKKQ
MDESKSFESV PIRNRLSDEE VARFAAQRYR FPGVEIKARL FRSYPYNELA SHVIGYIGRI
NQAEKAKIEE SEDSGNYRGT DYIGKLGVEQ SYEAQLHGTT GVQEMETSAG GRAVRRLNSS
QAVPGNSVVL SIDIKLQKLV EDLYGKRRGA LVALDPKTGE VLAFVSKPTF DPNLFVDGID
FENWQALNES PDKPLLNRAL RGTYPPGSTY KPFMALAALQ TGKRAEKTLI PDPGYFMFGN
HRFRDDKEGG HGMVDMYKSI VESCDTYYYT LARDMGVDLM YEQMKPLGFG QITGIDILGE
SRGVLPSTEW KRTTYKKPEQ QRWYSGETIS LGIGQGYNSF TMLQIAHATG TVANNGLKMK
PHLVREVVDV ETKVATLVAK EPVGQLPLTP ENLEVIKRGM VGVNIEGTSA SSFIGAQYVS
AGKTGTAQVY TVKQNEKYNA ANIDERMRDH ALFIAFAPAD DPKVALAMVV ENAGFGAQNA
APIARRVFDF VILGQYPALE DIEAVQKGQA TRPIGKPRPV ATVPWPPKSL EVDEALADKA
SLDLKAKR
//
