ID A0A1C4CB92_9GAMM Unreviewed; 649 AA.
AC A0A1C4CB92;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=GA0061081_10823 {ECO:0000313|EMBL:SCC16366.1};
OS Gilliamella bombicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Orbales; Orbaceae;
OC Gilliamella.
OX NCBI_TaxID=1798182 {ECO:0000313|EMBL:SCC16366.1, ECO:0000313|Proteomes:UP000199670};
RN [1] {ECO:0000313|Proteomes:UP000199670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-53248 {ECO:0000313|Proteomes:UP000199670};
RA Varghese N., Submissions Spin;
RL Submitted (AUG-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; FMAQ01000008; SCC16366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4CB92; -.
DR STRING; 1798182.GA0061081_10823; -.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199670; 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|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 Coiled coil {ECO:0000256|SAM:Coils};
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 Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 70..246
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 279..626
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT COILED 102..129
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 337
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 649 AA; 73374 MW; 110BBE9892254119 CRC64;
MITPISSKKK KTNIRDHSAE ANLFLRRALF SFIVIIILIV VLITKLADLQ ILNYGYYTTK
SNDNRIEIIP IPPNRGMIYD RNGTPLAINN ITYQLNIIPD KTKNLNEQLE ELKKIVDLTD
EDIETFQKER RNYRAHRPVP LKDNLTEKQI ARFVVDQHRF PFVSIVGIQH RYYPYGASLT
HILGYISKIN SQDKQRLEDE NKTSDYVATF NIGKMGIEKY YEEVLHGTPG YEKVEVNSRG
RIVRQLNQHP PQAGEDIYLS INLKLQLYIE QLLAGRKAAV VAIDPNNGEI LALVSSPSYD
SNPFVGGISS AKYSELLKDP SKPLFNRALL GAYPPASTVK PFISIAALSE GVISPKSVVN
DPGWWQLPGT ERRYRDWLKW GHGRVDVLKA IEESVDTYFY QVAYDMGIDR LNLWMTKFGY
GERTGIDISP NEETRAVMPS REWKMKRHKK SWLQGDTIPV GIGQGYWTAT PIQMAKALTT
LINNGKTYTP HFLLYKKSDI LNSSEHQPQV DSDNYIEKNS LVDVNPTYWS LAKEGMHRVM
FGSRGTARKV YADAKYQAAG KSGTAQVYGL KQDEIYNAHK IPERLRDHAL FIAYAPYDKP
KIALAIVLEN GGGGSSNGGA VARKILDFYL LGNNSTELDE SSSNTGIED
//
