ID K2JAS6_9GAMM Unreviewed; 621 AA.
AC K2JAS6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=B3C1_18381 {ECO:0000313|EMBL:EKE67624.1};
OS Gallaecimonas xiamenensis 3-C-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Gallaecimonas.
OX NCBI_TaxID=745411 {ECO:0000313|EMBL:EKE67624.1, ECO:0000313|Proteomes:UP000006755};
RN [1] {ECO:0000313|EMBL:EKE67624.1, ECO:0000313|Proteomes:UP000006755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-C-1 {ECO:0000313|EMBL:EKE67624.1,
RC ECO:0000313|Proteomes:UP000006755};
RX PubMed=23209203; DOI=10.1128/JB.01854-12;
RA Lai Q., Wang L., Wang W., Shao Z.;
RT "Genome Sequence of Gallaecimonas xiamenensis Type Strain 3-C-1.";
RL J. Bacteriol. 194:6937-6937(2012).
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:EKE67624.1}.
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DR EMBL; AMRI01000039; EKE67624.1; -; Genomic_DNA.
DR RefSeq; WP_008486695.1; NZ_AMRI01000039.1.
DR AlphaFoldDB; K2JAS6; -.
DR STRING; 745411.B3C1_18381; -.
DR PATRIC; fig|745411.4.peg.3614; -.
DR eggNOG; COG0768; Bacteria.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006755; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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|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:UP000006755};
KW Transferase {ECO:0000313|EMBL:EKE67624.1};
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 65..240
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 272..611
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 331
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 621 AA; 69839 MW; 610E028B5254440D CRC64;
MARKKVQIRD HGFEASLFWR RALFCLLVVV ACFGALIANL YHLQVKEFQN YQVRSNDNRI
KVVPVAPNRG IIYDRHGVVL AENRPIYSLE VVPEQVKSWD QPLADLQNLL GIDDDTISDF
RESLKGVRRF NRVPLLEELS EEQVALFSVN QYRFPGFSVE ARLKRFYPYA EALTHVLGYV
ARINDKDLQN LAEKDQLSNY AATHEIGKLG IERYYESTLH GQVGYMEVEV NNRGRVIRTL
RFEPPVPGKD LYLNLDLDLQ IKAQELLAGQ RGSIVAMDPN DGGILALASA PTYDPNLFVR
GISSKNYNAL LHSPDRPLIN RSTQGRYPPA STVKPFLALV GLEEGKITPA TKVWDPGFFE
LPNVNHKWRD WKRWGHGWVD LKRAIAESCD TYFYQLALDL GIDKIHDWMT LFGFGQYSGI
DIHEETSGVM PSRTWKERRF RQPWYIGDTI PIGIGQSYWT VTPVQLATAT SILANAGIYH
APRLLKATGS TTGTLNLPPD DKPRVQASAL HWREVENAML RTVQHVTGSA HKAFKDAPYS
AAGKTGTAQV VNIAQDERYD AQKVSERHRD NAMYVGYAPF EAPKIVVTVA LENIIGGGGS
VAAPLARQVM DHYLIEEAGG E
//
