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ID Q5LWC6_RUEPO Unreviewed; 379 AA.
AC Q5LWC6;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 08-MAY-2019, entry version 85.
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=mreD {ECO:0000313|EMBL:AAV93734.1};
GN Synonyms=mrdB {ECO:0000256|HAMAP-Rule:MF_02079}, rodA
GN {ECO:0000256|HAMAP-Rule:MF_02079};
GN OrderedLocusNames=SPO0416 {ECO:0000313|EMBL:AAV93734.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS (Silicibacter pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Ruegeria.
OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93734.1, ECO:0000313|Proteomes:UP000001023};
RN [1] {ECO:0000313|EMBL:AAV93734.1, ECO:0000313|Proteomes:UP000001023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT marine environment.";
RL Nature 432:910-913(2004).
RN [2] {ECO:0000313|EMBL:AAV93734.1, ECO:0000313|Proteomes:UP000001023}
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93734.1; -; Genomic_DNA.
DR RefSeq; WP_011046177.1; NC_003911.12.
DR STRING; 246200.SPO0416; -.
DR EnsemblBacteria; AAV93734; AAV93734; SPO0416.
DR KEGG; sil:SPO0416; -.
DR eggNOG; ENOG4105CNI; Bacteria.
DR eggNOG; COG0772; LUCA.
DR HOGENOM; HOG000282686; -.
DR KO; K05837; -.
DR OMA; HDYQKKR; -.
DR OrthoDB; 1133883at2; -.
DR BioCyc; RPOM246200:G1G48-423-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001023; 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; Q5LWC6.
DR SWISS-2DPAGE; Q5LWC6.
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:UP000001023};
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:UP000001023};
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 44 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_02079}.
FT TRANSMEM 56 76 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_02079}.
FT TRANSMEM 82 104 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_02079}.
FT TRANSMEM 116 134 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_02079}.
FT TRANSMEM 146 163 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_02079}.
FT TRANSMEM 175 207 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_02079}.
FT TRANSMEM 286 310 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_02079}.
FT TRANSMEM 322 346 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_02079}.
FT TRANSMEM 352 370 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_02079}.
SQ SEQUENCE 379 AA; 41206 MW; 539CEDB5CCB4C420 CRC64;
MSYLEYTVKS TPSGLRKILY MNWPLTLLLI SVASAGFLML YSVAGGSFSP WAEPQIKRFM
AGLVVMTAVA MVPIWFWRNM AAVAYGGSLV LLVMVELFGA VGMGAQRWID LGFMRLQPSE
LTKITLVMVL AAYYDWLPGK KTSRPLWVLV PVLIILVPTA LVLKQPDLGT AILLLSAGGA
LMFLAGVHWA YFAAVIAAGV GLITAVFKSR GTDWQLLKDY QFRRIDTFLD PSSDPLGAGY
HITQSKIALG SGGWSGRGFM QGTQSRLNFL PEKHTDFIFT TLAEEFGFIG GISLLSLYAL
IIAFCVATAL ATRDRFSSLV TLGIAVNFFL FFAVNMSMVM GLAPVVGVPL PMVSYGGSAM
LVLLVAFGLV HSAHIHRPR
//
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