ID S9ZB74_9RHOO Unreviewed; 668 AA.
AC S9ZB74;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=M622_05925 {ECO:0000313|EMBL:EPZ14520.1};
OS Thauera terpenica 58Eu.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=1348657 {ECO:0000313|EMBL:EPZ14520.1, ECO:0000313|Proteomes:UP000015455};
RN [1] {ECO:0000313|EMBL:EPZ14520.1, ECO:0000313|Proteomes:UP000015455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=58Eu {ECO:0000313|EMBL:EPZ14520.1,
RC ECO:0000313|Proteomes:UP000015455};
RA Liu B., Frostegard A.H., Shapleigh J.P.;
RT "Draft genome sequence of Thauera terpenica.";
RL Submitted (JUN-2013) 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:EPZ14520.1}.
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DR EMBL; ATJV01000081; EPZ14520.1; -; Genomic_DNA.
DR RefSeq; WP_021250474.1; NZ_ATJV01000081.1.
DR AlphaFoldDB; S9ZB74; -.
DR STRING; 1348657.M622_05925; -.
DR PATRIC; fig|1348657.5.peg.3074; -.
DR eggNOG; COG0768; Bacteria.
DR OrthoDB; 9789078at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000015455; 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:UP000015455};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 61..235
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 268..607
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 617..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 668 AA; 73760 MW; 47C92D2213663F62 CRC64;
MTEFRTPGRE LARFRLRVVV AMLFVCLCLG LLATRFYYLQ VLRHEYYLTR AEDNRIALLP
TVPHRGTIMD RNGVVLARNY ATYTLEITPD QVEDVEATLD ELATLVAIEA RDRRRFMKLL
EESRNFESVP VRSRLSDEEI ARIVSQRYRF PGVEVKARLL RDYPQGAVAS HIVGYIGRIN
QRDVERIEQA DNEANYRGSQ HIGKAGLELF YETELHGITG VEQVEVNAGG RAVRALSRIA
PIQGNDLELT LDIELQRVAE KAFGERRGAL VAIEPASGGV LALVSTPTFD PNLFVDGIST
QDWKALNDSP DHPLLNRAIY SAYPPGSTFK PFMALAGLEM GKRTARQAIA DIGYFNLGNH
RFMDDKIGGH GMVDLHKSIV VSCNTYYYQL AHELGIDNIA KFMGPLGFGS RTGIDLPGEA
SGVLPSPEWK RERFRRPEQQ QWYAGETISV GIGQGYNAYT PLQLASALAT LLNNGKQYRP
HIVRHVVDSL SGERRAVERE PVREIPLKPA NVKAVLDGMV GVNSEGTGRR AFQGAAYTSG
GKTGTAQVFS LRGQRYEEKR LRERLRDHSW FIAYAPAQAP QIALAVLVEN GGFGAQSAAP
IARQVMDYYL LHQRAGGPAA EDAEADEADE SVDAGPKDEE VVEPAAEPGL PARGAARSPA
PAAGRRAQ
//
