(data stored in SCRATCH zone)

SWISSPROT: E6V287_VARPE

ID   E6V287_VARPE            Unreviewed;       656 AA.
AC   E6V287;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 45.
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   OrderedLocusNames=Varpa_0296 {ECO:0000313|EMBL:ADU34518.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34518.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34518.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34518.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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;
CC         Evidence={ECO:0000256|HAMAP-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}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02081}.
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DR   EMBL; CP002417; ADU34518.1; -; Genomic_DNA.
DR   RefSeq; WP_013538764.1; NC_014931.1.
DR   STRING; 595537.Varpa_0296; -.
DR   EnsemblBacteria; ADU34518; ADU34518; Varpa_0296.
DR   GeneID; 29719799; -.
DR   KEGG; vpe:Varpa_0296; -.
DR   eggNOG; ENOG4105CJN; Bacteria.
DR   eggNOG; COG0768; LUCA.
DR   HOGENOM; HOG000266120; -.
DR   KO; K05515; -.
DR   OMA; SCDTYYY; -.
DR   OrthoDB; 423699at2; -.
DR   BioCyc; VPAR595537:G1GQO-298-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008917; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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:0016757; F:transferase activity, transferring glycosyl groups; 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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56519; SSF56519; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR03423; pbp2_mrdA; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6V287.
DR   SWISS-2DPAGE; E6V287.
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   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Glycosyltransferase {ECO:0000313|EMBL:ADU34518.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Membrane {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:UP000008917};
KW   Transferase {ECO:0000313|EMBL:ADU34518.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT   TRANSMEM     18     38       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02081}.
FT   DOMAIN       62    237       PBP_dimer. {ECO:0000259|Pfam:PF03717}.
FT   DOMAIN      270    608       Transpeptidase. {ECO:0000259|Pfam:
FT                                PF00905}.
FT   ACT_SITE    329    329       Acyl-ester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02081}.
SQ   SEQUENCE   656 AA;  71808 MW;  D4F38E17729A8D3F CRC64;
     MTEIRNVAAD LARFKRRVIV IGLAVLFAFG LLSSRLIYLQ VTRHEDLAEQ AESNRTAIVP
     VVPNRGLILD RNGIVLASNY SAYTLEITPS KVNDVEETID NLTQVLEVSP RDRRRFKRLR
     EDSRSFDSIP IRTRLSDEEV ARFAAQRYRF PGVEIKARLF RNYPNGETGA HVLGYIGRIN
     QREKTAMEDW EEEEQANYKG TDYIGKLGIE QSYEKTLHGQ TGVEQMETSA GGRAIRRLAS
     HPATPGNTVM LSLDIKLQKL VEDMFGDRRG ALVAIDPKTG EVLAFVSKPT FDPNLFVEGI
     DTESWKELSE SLDKPLLNRA LRGTYPPGST YKPFMALAAL QTGKRGASVV VNDPGYFNFG
     GHRFGSPEGN LGGVDMRRSI QLSSNIYYYS LANEMGVDLI HDFMKPLGFG QITGIDLGGE
     VRGVLPSTEW KRNAYKRPEQ KKWYAGETIS LGIGQGYNTF TMLQLAQATA IVADGGIKRK
     PHLVLATRNT VSGQVVPLPQ PPPENLGYTA ANVAVIREGL TSVVTSGTAR SVFAGAGYQA
     AGKTGTAQAV TQAQNTKYNA RALEEHQRDH ALFMAFAPVS DPKIAVAVIV ENAGWGAGAA
     APIARRVFDY WLMDQYPSEA DMAAIKIGKA GAPMGKPRVA SEVAWPVATT TPATAP
//

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