(data stored in SCRATCH zone)

SWISSPROT: Q146Z1_PARXL

ID   Q146Z1_PARXL            Unreviewed;       382 AA.
AC   Q146Z1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Peptidoglycan glycosyltransferase MrdB {ECO:0000256|HAMAP-Rule:MF_02079};
DE            Short=PGT {ECO:0000256|HAMAP-Rule:MF_02079};
DE            EC=2.4.1.129 {ECO:0000256|HAMAP-Rule:MF_02079};
DE   AltName: Full=Cell elongation protein RodA {ECO:0000256|HAMAP-Rule:MF_02079};
DE   AltName: Full=Cell wall polymerase {ECO:0000256|HAMAP-Rule:MF_02079};
DE   AltName: Full=Peptidoglycan polymerase {ECO:0000256|HAMAP-Rule:MF_02079};
DE            Short=PG polymerase {ECO:0000256|HAMAP-Rule:MF_02079};
GN   Name=mrdB {ECO:0000256|HAMAP-Rule:MF_02079};
GN   Synonyms=rodA {ECO:0000256|HAMAP-Rule:MF_02079};
GN   ORFNames=Bxe_A4402 {ECO:0000313|EMBL:ABE28598.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28598.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28598.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28598.1,
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: Peptidoglycan polymerase that is essential for cell wall
CC       elongation. {ECO:0000256|HAMAP-Rule:MF_02079}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-
CC         D-Ala)](n)-diphospho-di-trans,octa-cis-undecaprenol + beta-D-
CC         GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC         diphospho-di-trans,octa-cis-undecaprenol = [GlcNAc-(1->4)-
CC         Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-diphospho-
CC         di-trans-octa-cis-undecaprenol + di-trans,octa-cis-undecaprenyl
CC         diphosphate + H(+); Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602,
CC         Rhea:RHEA-COMP:9603, ChEBI:CHEBI:15378, ChEBI:CHEBI:58405,
CC         ChEBI:CHEBI:60033, ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02079};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02079}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02079}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02079}.
CC   -!- SIMILARITY: Belongs to the SEDS family. MrdB/RodA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02079}.
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DR   EMBL; CP000270; ABE28598.1; -; Genomic_DNA.
DR   RefSeq; WP_011486456.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4402; -.
DR   EnsemblBacteria; ABE28598; ABE28598; Bxe_A4402.
DR   GeneID; 4005134; -.
DR   KEGG; bxb:DR64_2077; -.
DR   KEGG; bxe:Bxe_A4402; -.
DR   PATRIC; fig|266265.5.peg.61; -.
DR   eggNOG; ENOG4105CNI; Bacteria.
DR   eggNOG; COG0772; LUCA.
DR   HOGENOM; HOG000282686; -.
DR   KO; K05837; -.
DR   OMA; HDYQKKR; -.
DR   OrthoDB; 1133883at2; -.
DR   BioCyc; BXEN266265:BXE_RS00300-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:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:InterPro.
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_02079; PGT_RodA; 1.
DR   InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR   InterPro; IPR001182; FtsW/RodA.
DR   InterPro; IPR011923; RodA/MrdB.
DR   PANTHER; PTHR30474; PTHR30474; 1.
DR   PANTHER; PTHR30474:SF1; PTHR30474:SF1; 1.
DR   Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR   TIGRFAMs; TIGR02210; rodA_shape; 1.
DR   PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q146Z1.
DR   SWISS-2DPAGE; Q146Z1.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02079};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02079};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02079};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02079};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_02079};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_02079,
KW   ECO:0000256|SAAS:SAAS00176820};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02079};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02079};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02079,
KW   ECO:0000256|SAAS:SAAS00176858};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02079,
KW   ECO:0000256|SAAS:SAAS00176861}.
FT   TRANSMEM     23     41       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM     77     97       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    139    156       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    162    180       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    185    203       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    286    307       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    319    346       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    352    374       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
SQ   SEQUENCE   382 AA;  41796 MW;  BD52D51E6DBB064D CRC64;
     MQFDKRAWLD RIKRMFAGFD RPLALIVFLL LCVGIVTLYS ASLDVPGRVE DQLRNIMLTF
     VLMWALANVP PTTLMRFAVP LYTFGIALLV AVALFGLTRK GAKRWINVGV VIQPSEILKI
     ATPLMLAWYY QRREGVMRWY DFLVGLLILA VPVGLIAKQP DLGTAVLVFA AGFFVIYFAG
     LSFKLIVPVL IAGVIAVGSI AAFQDKICQP EVQWPLMHDY QKHRICTLLD PTSDPLGKGF
     HTIQAVIAIG SGGAFGKGWL KGTQAHLEFI PEKHTDFIFA VFSEEFGLAG GIVLLTLYML
     LIARGLYIAA NGATLFGRLL AGSLTMAFFT YAFVNIGMVS GILPVVGVPL PFMSYGGTAL
     TTLGVAIGLI MSIARQKRLM QS
//

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