ID A0A0Q5ZHZ5_9BURK Unreviewed; 709 AA.
AC A0A0Q5ZHZ5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=ASG30_21475 {ECO:0000313|EMBL:KQT12990.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT12990.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT12990.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT12990.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT12990.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT12990.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass 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:KQT12990.1}.
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DR EMBL; LMQL01000006; KQT12990.1; -; Genomic_DNA.
DR RefSeq; WP_055893873.1; NZ_LMQL01000006.1.
DR AlphaFoldDB; A0A0Q5ZHZ5; -.
DR STRING; 1736365.ASG30_21475; -.
DR OrthoDB; 9789078at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051173; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000051173};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT DOMAIN 61..238
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 271..610
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 632..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 330
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 709 AA; 76918 MW; E39AAA48E4DD9313 CRC64;
MTELRNVEAD LSRFRTRVLA ASLAVLACFL LLALRLAYLQ VVRHDELDEQ AESNRTAIVP
IVPNRGLILD RNGVVLATNY SAYTLEITPS RLAHTLERTI DDLAQVVEIQ ARDRRRFKKL
LEESKSFESL PIRTKLTDEE VARFAAQRFR FPGVEIKARL FRNYPYGELA SHVIGYIGRI
NQAEKKQMEE WDEEDQANYR GTEYIGKLGV EQSLEKQLHG LTGVEQVETS AGGRAVRKLA
SKPATPGNTV MLSIDIRMQK MVEDMYGDRR GALVALDPKT GEVLAFVSKP TFDPGLFVDG
IDSENWQALN ESIEKPLLNR ALRGTYPPGS TYKPFMALAA LTTGKRSATQ VVMDGGSWSF
GGHVFRSHGD HGLGAVDMHT SIVKSSNVYY YSLANEMGVD LMHDFMKPLG FGQLTGIDIF
GEVRGVLPSQ EWKRNYYRRP EQKKWYAGET ISLGIGQGYN SFTMLQLAQA TATVVNNGVK
HKPRLVIATQ DPMTREQTLV PAQPPEDLGY KPEHVAVIRK AMVGVTQGGT STRVFAGAGY
LSGGKTGTAQ AVTIGQKEKY NASKLEEHQR DHSLYIAFAP ADDPKIALAA VVENSGFGAA
AAAPIARRVF DYWLMGLYPT DEDMAAVRKG QAAAPVGKPR PAAEVGWPPA GSGGAASPMP
AASAASVAAT PAATPASAPV AQPKPASAPA RAIASIPAAS ALPVNARAN
//
