(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWC6_RUEPO

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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