ID A0A0A3B8H7_9PAST Unreviewed; 635 AA.
AC A0A0A3B8H7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=OA57_09740 {ECO:0000313|EMBL:KGQ69899.1};
OS Chelonobacter oris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Chelonobacter.
OX NCBI_TaxID=505317 {ECO:0000313|EMBL:KGQ69899.1, ECO:0000313|Proteomes:UP000030380};
RN [1] {ECO:0000313|EMBL:KGQ69899.1, ECO:0000313|Proteomes:UP000030380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1662 {ECO:0000313|EMBL:KGQ69899.1,
RC ECO:0000313|Proteomes:UP000030380};
RA Kudirkiene E., Hansen M.J., Bojesen A.M.;
RT "Draft genome sequence of Chelonobacter oris 1662T, associated with
RT respiratory disease in Hermann's Tortoises.";
RL Submitted (NOV-2014) 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:KGQ69899.1}.
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DR EMBL; JSUM01000014; KGQ69899.1; -; Genomic_DNA.
DR RefSeq; WP_034616977.1; NZ_LEKK01000011.1.
DR AlphaFoldDB; A0A0A3B8H7; -.
DR STRING; 505317.OA57_09740; -.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000030380; 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 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:UP000030380};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 63..238
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 270..609
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 329
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 635 AA; 71921 MW; 1FE7414516DE7009 CRC64;
MAKEIIRDNK AEQNLFLRRV LVAFIGVLLL LSVLLLNNYN LQVRDYDNYQ TRSNGNRIKL
LPVAPTRGLI YDRNNRVLAE NLTFFGLYIV PEKTENLQQT YDELRQIVGL SDEDIEAFTK
ERRRNSRYTP ILLKSDLTEE QIARFSVNQH LFPSLEIRPY FKRHYPYGED LTHILGYVAK
INDKDVERLK EEDKLANYAG TGDIGKLGIE RYYEEQLHGE VGFEEVEVNN RGKVIRTLRQ
QPAVSGKSIK LTIDLTLQRY IRQLLDGRRG AVVVLDPRDN SILAMVSSPS YDNNLFVGGI
SSANYNALLN NPERPLYSRT TQGAFPPAST VKPFIAVAAL QDGIITTNST IYDPGYWVLP
GTDRRYRDWL RSGHGRLNLN KAIMESADTY FYQLIYDMGI NRFSDWMKRF GFGMPTGVDI
REETSGVMPT REWKQQRYKK PWVIGDTIPV GIGQGYWTAT PLQLTKALSV LINNGRVDTP
HFMQEVIGNE TQPYQDPKLY DDISGVPQAY WNAAKAGMYS VLYGNTGTAK KAFSNMSYLA
AGKSGTAQVF GLKENQKYDA SNLASHLHDH AWFIAYAPYN NPTIALSVFL ENAGGGSSQA
APIARSIMDY YLLNMGNLQQ SAVADNLKQT DKVVR
//
