ID A0A099PBM8_9GAMM Unreviewed; 629 AA.
AC A0A099PBM8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, 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=LH51_14935 {ECO:0000313|EMBL:KGK41436.1};
OS Nitrincola sp. A-D6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK41436.1, ECO:0000313|Proteomes:UP000029924};
RN [1] {ECO:0000313|EMBL:KGK41436.1, ECO:0000313|Proteomes:UP000029924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-D6 {ECO:0000313|EMBL:KGK41436.1,
RC ECO:0000313|Proteomes:UP000029924};
RA Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C.,
RA Fernandez S., Ferrer A., Chavez R., Levican G.;
RT "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola sp.
RT Strain A-D6 Isolated from a Salt Flat in Northern Chile.";
RL Submitted (SEP-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:KGK41436.1}.
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DR EMBL; JRLB01000090; KGK41436.1; -; Genomic_DNA.
DR RefSeq; WP_036523383.1; NZ_JRLB01000090.1.
DR AlphaFoldDB; A0A099PBM8; -.
DR STRING; 1545442.LH51_14935; -.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000029924; 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:UP000029924};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 64..234
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 269..615
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 327
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 629 AA; 70513 MW; F6CD36F68DA82148 CRC64;
MQQAETLKDY SREAQTFKRR ALLAFVIVVL AFMLLIGRVY FLQVIEYERY AAISDRNRIQ
LQPVAPRRGL IYDRQGVLLA DNQPTFSVTL LREEIRDMDE TLAALAELIE ISERDVERFR
VRLQQRRRPY ESVPLRFRLT EEEIAKISVN YHMLPGVQVE ADLIRYYPYG ESLAHVVGYV
GRINERDLQT LDPVKYAGTN YLGKLGVERF YEPILHGNVG SRKVETNARG RVLRILEQND
PAPGADIKLS LDLRLQQFTE KLLEGRRASV VALDPKTGGI LALVSTPAYD PNLFVMGISN
TDYDALRDDV DLPLFNRAVR GGYPPGSTIK PIMALAAIDS GSVSPDYTIW DPGYYQITPG
GRRYRDWRRG GHGRVNMNLA IAQSVDTWFY DVGHRMGNEP MARYMRMFGF GEITTLDTPE
AIRGVLPTAD WKRGSLGEPW YPGDSVNMSI GQGFVVATPL QLAVAANVLA NRGKWQQPRL
LMGTVEETDA GEVLTLPDLV NEHPVPDDIK VKNPEFWDQI IQGMVDVMHG PTGTARRVGQ
GMEYKMAGKT GTAQVVAIPD DGRYKPEELS ERHHDHALFI AFAPADDPQI ALAVVVENGG
GGSSVAAPIA RKVMDAWLLD RYELEAEDE
//
