ID Z9JLV1_9GAMM Unreviewed; 687 AA.
AC Z9JLV1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=AF72_04015 {ECO:0000313|EMBL:EWS78742.1};
OS Xylella taiwanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=1444770 {ECO:0000313|EMBL:EWS78742.1, ECO:0000313|Proteomes:UP000020406};
RN [1] {ECO:0000313|EMBL:EWS78742.1, ECO:0000313|Proteomes:UP000020406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLS229 {ECO:0000313|EMBL:EWS78742.1,
RC ECO:0000313|Proteomes:UP000020406};
RX PubMed=24652975;
RA Su C.C., Deng W.L., Jan F.J., Chang C.J., Huang H., Chen J.;
RT "Draft Genome Sequence of Xylella fastidiosa Pear Leaf Scorch Strain in
RT Taiwan.";
RL Genome Announc. 2:e00166-14(2014).
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:EWS78742.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JDSQ01000005; EWS78742.1; -; Genomic_DNA.
DR RefSeq; WP_038270715.1; NZ_VOSE01000002.1.
DR AlphaFoldDB; Z9JLV1; -.
DR STRING; 1444770.AF72_04015; -.
DR GeneID; 69682487; -.
DR KEGG; xtw:AB672_03615; -.
DR PATRIC; fig|1444770.3.peg.976; -.
DR eggNOG; COG0768; Bacteria.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000020406; 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 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 66..234
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 267..604
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 326
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 687 AA; 75597 MW; 873ADC51126B05FA CRC64;
MNVPHPQAKH TYAEVEQFRR RALLSLFFVM VCLFGLVAWY FKLQVLDHEI YATRSDANRI
KLHPVVPGRG MIYDRDGRLL ADNVPAFRLD VMPDKVDDME AMLVELGKVI PLSADELERF
HRERKVRRRF MPVTLKLRMS EEERARFAVD RWRFPGVELE PYLTRRYPYG DLFAHVIGYV
GRIDEKDLEV LKGGDVALTY IGKSGLERYY EQVLRGRIGY QQIETNVQGR AIRSLGQVTA
QAGADLRLSI DADLQRAMVA AFGQYEGAAV AMDPRTGEIL GMVSLPSYDP NLFVNGISHA
QFDALNADPS RPQFNRLVSG GVAPGSTLKP LIALAGLDAG VRRPEDRILS TGMFYLPGVN
RGWGDAHRGG HGWTDLRKSI AQSVNTYYYK LALDLGIERF TDYMRRYGLG QLTGIDLTGE
ISGILPSLEY KRKVRKQAWY QGDTVNVSIG QGDWKVTLLQ LVRSVAGLAS GQMNRPHLVV
AERTGFSQPW QVLAQPASQP ISPNPANVQV VREGMIDTMR PGGTGYQAAV GAPYSIAGKT
GTAQVASRKG TAAVDPRNLP MHLRHRALFV GFAPADNPTI AVAIAVEGGG YGASTAAPIA
RKIFDAWLLG KLPEGLEPLD SARGRTAIGL TQFDTTVAEV CEAGNRAALQ LGELQVSVAA
WMLNSASMMP AVPRAPVMLD PSQEEDP
//
