RODA_HELPJ
ID RODA_HELPJ Reviewed; 381 AA.
AC Q9ZLA0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Peptidoglycan glycosyltransferase MrdB {ECO:0000255|HAMAP-Rule:MF_02079};
DE Short=PGT {ECO:0000255|HAMAP-Rule:MF_02079};
DE EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_02079};
DE AltName: Full=Cell elongation protein RodA {ECO:0000255|HAMAP-Rule:MF_02079};
DE AltName: Full=Cell wall polymerase {ECO:0000255|HAMAP-Rule:MF_02079};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000255|HAMAP-Rule:MF_02079};
DE Short=PG polymerase {ECO:0000255|HAMAP-Rule:MF_02079};
GN Name=mrdB {ECO:0000255|HAMAP-Rule:MF_02079}; Synonyms=rodA;
GN OrderedLocusNames=jhp_0680;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell wall
CC elongation. {ECO:0000255|HAMAP-Rule:MF_02079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02079};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02079}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02079}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02079}.
CC -!- SIMILARITY: Belongs to the SEDS family. MrdB/RodA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02079}.
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DR EMBL; AE001439; AAD06247.1; -; Genomic_DNA.
DR PIR; F71903; F71903.
DR AlphaFoldDB; Q9ZLA0; -.
DR SMR; Q9ZLA0; -.
DR STRING; 85963.jhp_0680; -.
DR EnsemblBacteria; AAD06247; AAD06247; jhp_0680.
DR KEGG; hpj:jhp_0680; -.
DR eggNOG; COG0772; Bacteria.
DR OMA; HDYQKKR; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000804; 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 PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..381
FT /note="Peptidoglycan glycosyltransferase MrdB"
FT /id="PRO_0000062719"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
SQ SEQUENCE 381 AA; 42943 MW; 4DF6C470CCA353E1 CRC64;
MALDKRIWMH FDLLPFVFII PLLVVSFLLI FESSAVLSLK QGVYYAIGFL LFWVVFFIPF
RKLDRWLFAL YWACVILLAL VDFMGSSKLG AQRWLVIPFT SITLQPSEPV KIAILLLLAH
LIKINPPPFK GYDWGMFLKL SFYICLPAAL ILKQPDLGTA LIVLIMGFGI LLIVGLRTRV
WLPLLIALIV ASPIAYHFLH DYQKKRIADF LSEKPNYHVM QSIIAIGSGG FLGKSKEACT
QTKFKFLPIA TSDFIFAYFV ERFGFLGAIL LFAIYIGLSL HLFFYLFESN SDWFLKIVAL
GISILIFVYS SVNIAMTLGL APVVGIPLPL FSYGGSSFIT FMILFAILEN LLAFRYIFGN
NSKPSFGNFG FLAQLVRALG S
