RODA_HELPY
ID RODA_HELPY Reviewed; 381 AA.
AC P56098;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, 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=HP_0743;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07794.1; -; Genomic_DNA.
DR PIR; G64612; G64612.
DR RefSeq; NP_207537.1; NC_000915.1.
DR RefSeq; WP_010875539.1; NC_018939.1.
DR AlphaFoldDB; P56098; -.
DR SMR; P56098; -.
DR STRING; 85962.C694_03820; -.
DR PaxDb; P56098; -.
DR EnsemblBacteria; AAD07794; AAD07794; HP_0743.
DR KEGG; hpy:HP_0743; -.
DR PATRIC; fig|85962.47.peg.792; -.
DR eggNOG; COG0772; Bacteria.
DR OMA; HDYQKKR; -.
DR PhylomeDB; P56098; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..381
FT /note="Peptidoglycan glycosyltransferase MrdB"
FT /id="PRO_0000062718"
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 99..119
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; 43136 MW; ACF415F939D746CA CRC64;
MALDKRIWMH FDLLPFVFII PLLVVSFLLI FESSAVLSLK QGVYYAIGFI LFWIVFFIPF
RKLGRWLFVF YWACVILLAL VDFMGYSKLG AQRWLVIPFI SITLQPSEPV KIAILLLLAH
LIKINPPPFK GYDWGMFLKL SFYICLPAAL ILKQPDLGTA LIVLIMGFGI LLIVGLRTRV
WLPLFIALLV ASPIAYHFLH DYQKKRIADF LSEKPNYHVM QSIIAIGSGG FLGKSKEACT
QTKFKFLPIA TSDFIFAYFV ERFGFLGAML LFAIYIGLSL HLFFYLFESN SDWFLKIVAL
GISILIFVYS SVNIAMTLGL APVVGIPLPL FSYGGSSFIT FMILFGILEN LLAFRYIFGY
NSKPSFGNFG FLAQLVRALG S
