ID A0A160N4M1_9GAMM Unreviewed; 657 AA.
AC A0A160N4M1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=ATSB10_34360 {ECO:0000313|EMBL:AND70890.1};
OS Dyella thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=445710 {ECO:0000313|EMBL:AND70890.1, ECO:0000313|Proteomes:UP000077255};
RN [1] {ECO:0000313|EMBL:AND70890.1, ECO:0000313|Proteomes:UP000077255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATSB10 {ECO:0000313|EMBL:AND70890.1,
RC ECO:0000313|Proteomes:UP000077255};
RA Lee Y., Hwangbo K., Chung H., Yoo J., Kim K.Y., Sa T.M., Um Y.,
RA Madhaiyan M.;
RT "Complete genome sequencing and analysis of ATSB10, Dyella thiooxydans
RT isolated from rhizosphere soil of sunflower (Helianthus annuus L.).";
RL Submitted (FEB-2016) 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; CP014841; AND70890.1; -; Genomic_DNA.
DR RefSeq; WP_063673866.1; NZ_CP014841.1.
DR AlphaFoldDB; A0A160N4M1; -.
DR STRING; 445710.ATSB10_34360; -.
DR KEGG; dtx:ATSB10_34360; -.
DR PATRIC; fig|445710.3.peg.3435; -.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000077255; Chromosome.
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|ARBA:ARBA00022645, ECO:0000256|HAMAP-
KW Rule:MF_02081}; 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:UP000077255};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 21..47
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 71..239
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 273..615
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 628..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..657
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 657 AA; 71575 MW; C611BB6410557E94 CRC64;
MSKRRIHRPR RAIKDPRGES ALFRGRAVAG FALILLGLLA LVGRYAFLQV LHHDEFATRS
DANRIKPRAL QPARGLIYDR NGVLLADNVP AFRLEVVPEQ VPDMKAMLAQ IGSVVPLGDD
DIDAFKKQLA QSRRFDSIPL KMHLSEDDIA RFSVNRWRFP GVDVVPYLTR RYTFGPRFAH
VIGYVNRIDD NDLKRLDPVR YKGATHVGRS GIERSYEDLL HGTPGYELVE VNADGRTQRV
LETHPPIPGK NLYLSIDARI QKAAEDAFAG RPGAAVAIDP RNGQVLAMVS VPSFDPNLFV
NGISSADYKA LTTDPKKPLY NRALRGVYPP GSTVKPLIGL AGLESGLRTP DDTVVSTGQY
CIPGTTFCRR DDQRGGAGRV DLAEAIEQSV NTYFYKLALD LGIDRLSHYM SQFGFGHATG
IDLVGESDGV LPSREWKAAH SKMPWFPGET MIAGIGQGYW AVTPLQLAHA IATFAGGGVP
YKPRLVMATQ DGVDAKAVPL PNPPEGPSLI SSKANWEAID KGMEMVMYGD KGTGRSLTVG
FPYRIAGKSG TAQRYSRTGN SYDDRSNLAY LASRNRAWFE MYAPADDPQI AVAVVLEAGA
WGSSSAGPIA RHILDAWLAT KGSKAPPFTP YSDPSLGDVP PLPPEDLPVA PPDGDTP
//
