(data stored in ACNUC10821 zone)

SWISSPROT: C8U2Z6_ECO10

ID   C8U2Z6_ECO10            Unreviewed;       370 AA.
AC   C8U2Z6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 57.
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   ECO:0000313|EMBL:BAI29504.1};
GN   Synonyms=rodA {ECO:0000256|HAMAP-Rule:MF_02079};
GN   OrderedLocusNames=ECO103_0641 {ECO:0000313|EMBL:BAI29504.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29504.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29504.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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; AP010958; BAI29504.1; -; Genomic_DNA.
DR   RefSeq; WP_000131719.1; NC_013353.1.
DR   EnsemblBacteria; BAI29504; BAI29504; ECO103_0641.
DR   KEGG; eoh:ECO103_0641; -.
DR   HOGENOM; HOG000282686; -.
DR   KO; K05837; -.
DR   OMA; HDYQKKR; -.
DR   BioCyc; ECOL585395:ECO103_RS03345-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000959; Chromosome.
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; C8U2Z6.
DR   SWISS-2DPAGE; C8U2Z6.
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:UP000000959};
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   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     20     38       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM     50     68       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM     74     95       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    136    154       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    160    176       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    183    202       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    263    289       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    310    332       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
FT   TRANSMEM    338    359       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02079}.
SQ   SEQUENCE   370 AA;  40476 MW;  68FCDF8D6B123D69 CRC64;
     MTDNPNKKTF WDKVHLDPTM LLILLALLVY SALVIWSASG QDIGMMERKI GQIAMGLVIM
     VVMAQIPPRV YEGWAPYLYI ICIILLVAVD AFGAISKGAQ RWLDLGIVRF QPSEIAKIAV
     PLMVARFINR DVCPPSLKNT GIALVLIFMP TLLVAAQPDL GTSILVALSG LFVLFLSGLS
     WRLIGVAVVL VAAFIPILWF FLMHDYQRQR VMMLLDPESD PLGAGYHIIQ SKIAIGSGGL
     RGKGWLHGTQ SQLEFLPERH TDFIFAVLAE ELGLVGILIL LALYILLIMR GLWIAARAQT
     TFGRVMAGGL MLILFVYVFV NIGMVSGILP VVGVPLPLVS YGGSALIVLM AGFGIVMSIH
     THRKMLSKSV
//

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