(data stored in ACNUC7421 zone)

SWISSPROT: Q146Z0_PARXL

ID   Q146Z0_PARXL            Unreviewed;       767 AA.
AC   Q146Z0;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 75.
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=Bxe_A4401 {ECO:0000313|EMBL:ABE28599.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28599.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28599.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28599.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE28599.1; -; Genomic_DNA.
DR   RefSeq; WP_011486457.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4401; -.
DR   EnsemblBacteria; ABE28599; ABE28599; Bxe_A4401.
DR   GeneID; 4005135; -.
DR   KEGG; bxb:DR64_2076; -.
DR   KEGG; bxe:Bxe_A4401; -.
DR   PATRIC; fig|266265.5.peg.62; -.
DR   eggNOG; ENOG4105CJN; Bacteria.
DR   eggNOG; COG0768; LUCA.
DR   HOGENOM; HOG000266120; -.
DR   KO; K05515; -.
DR   OMA; SCDTYYY; -.
DR   OrthoDB; 423699at2; -.
DR   BioCyc; BXEN266265:BXE_RS00305-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001817; Chromosome 1.
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; Q146Z0.
DR   SWISS-2DPAGE; Q146Z0.
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:UP000001817};
KW   Glycosyltransferase {ECO:0000313|EMBL:ABE28599.1};
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:UP000001817};
KW   Transferase {ECO:0000313|EMBL:ABE28599.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT   TRANSMEM     21     42       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02081}.
FT   DOMAIN       61    251       PBP_dimer. {ECO:0000259|Pfam:PF03717}.
FT   DOMAIN      283    622       Transpeptidase. {ECO:0000259|Pfam:
FT                                PF00905}.
FT   ACT_SITE    342    342       Acyl-ester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02081}.
SQ   SEQUENCE   767 AA;  82387 MW;  5BD695CFA3CCEEA6 CRC64;
     MTEFKDTQQQ LSKFRLRVAA AGLFVFVCFG LIGFRFLFLQ VWHYSKYSLQ ADENRISVAP
     IVPNRGIITD RNGVVLAKNY SAYTLEITPS KLNDSLENVI DNLATVVSID ARDRRRFKKL
     QEDSKNFESL PIRTRLTDDE VARFTAQRFR FPGVEVRARL FRQYPLGPTA AHVIGYIGRI
     SQRDQDRIDD ASDQNDSDPD HYDPRLDANN YKGTDYIGKI GVEQSYETEL HGQTGFEEVE
     VTAGGRPVRT LSRTQATPGN NLVLSLDIGL QQVAEQAFAG RRGALVAIEP SSGDVLAFVS
     APSFDPNSFV DGIDQQTWDD LNNSPDHPLL NRPLHGTYPP GSTYKPFMAL AALTLHKRTP
     GWGFQDPGSY TFGGHTFRND VRSGQGWVDM NRAIVVSNDT YFYMLAHDLG VNNIANFMKP
     WGFGQITGID ISGEARGILP STEWKRKAYR KPEQQRWYEG ETISLGIGQG YNSFTILQLA
     HATATLANNG VVMKPHLVRD IENPITKETR PVVRDPSDRI AVKQSDIDII KRAMVGVVTN
     GTASKLFVGA PYQAAGKTGT AQVYSLQGAN YKGHAIAEHL RDHALFIAFA PAEQPKIALA
     LIVENGGWGA EAAGPIARKV LDYYLVGKNK PGAQAAAIEA AASATEDASA PEVGGAPAPQ
     EAVQPVKVAA GFTALPIPGA ASAAEAASAA AAASAASAAS ASASAAASAP VAASTSAAAK
     NPTPRKSGAP HKPRPASEPA PSAAAPSRDD GIQATSPRQP VSGGIDE
//

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