RODA_ECOLI
ID RODA_ECOLI Reviewed; 370 AA.
AC P0ABG7; P13409; P15035;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Peptidoglycan glycosyltransferase MrdB {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000305};
DE Short=PGT {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000305};
DE EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000269|PubMed:27643381};
DE AltName: Full=Cell elongation protein RodA {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000305};
DE AltName: Full=Cell wall polymerase {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000305};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000303|PubMed:27643381};
DE Short=PG polymerase {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000303|PubMed:27643381};
DE AltName: Full=Rod shape-determining protein {ECO:0000305};
GN Name=mrdB {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000303|PubMed:6243629};
GN Synonyms=rodA {ECO:0000303|PubMed:6348029};
GN OrderedLocusNames=b0634, JW0629;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=2644207; DOI=10.1128/jb.171.1.558-560.1989;
RA Matsuzawa H., Asoh S., Kunai K., Muraiso K., Takasuga A., Ohta T.;
RT "Nucleotide sequence of the rodA gene, responsible for the rod shape of
RT Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding
RT protein 2, constitute the rodA operon.";
RL J. Bacteriol. 171:558-560(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 355-370.
RX PubMed=3316191; DOI=10.1128/jb.169.12.5692-5699.1987;
RA Takase I., Ishino F., Wachi M., Kamata H., Doi M., Asoh S., Matsuzawa H.,
RA Ohta T., Matsuhashi M.;
RT "Genes encoding two lipoproteins in the leuS-dacA region of the Escherichia
RT coli chromosome.";
RL J. Bacteriol. 169:5692-5699(1987).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=6243629; DOI=10.1128/jb.141.1.52-57.1980;
RA Tamaki S., Matsuzawa H., Matsuhashi M.;
RT "Cluster of mrdA and mrdB genes responsible for the rod shape and
RT mecillinam sensitivity of Escherichia coli.";
RL J. Bacteriol. 141:52-57(1980).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=6348029; DOI=10.1128/jb.155.2.854-859.1983;
RA Stoker N.G., Pratt J.M., Spratt B.G.;
RT "Identification of the rodA gene product of Escherichia coli.";
RL J. Bacteriol. 155:854-859(1983).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=27643381; DOI=10.1038/nmicrobiol.2016.172;
RA Cho H., Wivagg C.N., Kapoor M., Barry Z., Rohs P.D., Suh H., Marto J.A.,
RA Garner E.C., Bernhardt T.G.;
RT "Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase
RT families functioning semi-autonomously.";
RL Nat. Microbiol. 2016:16172-16172(2016).
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell wall
CC elongation (PubMed:27643381). Also required for the maintenance of the
CC rod cell shape (PubMed:2644207). Functions probably in conjunction with
CC the penicillin-binding protein 2 (mrdA) (PubMed:2644207,
CC PubMed:27643381). {ECO:0000269|PubMed:2644207,
CC ECO:0000269|PubMed:27643381}.
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, ECO:0000269|PubMed:27643381};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000269|PubMed:27643381}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02079, ECO:0000269|PubMed:6348029}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02079}.
CC -!- DISRUPTION PHENOTYPE: At 42 degrees Celsius, mutation causes formation
CC of spherical cells and mecillinam resistance.
CC {ECO:0000269|PubMed:6243629}.
CC -!- SIMILARITY: Belongs to the SEDS family. MrdB/RodA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000305}.
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DR EMBL; M22857; AAA24571.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40834.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73735.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35277.1; -; Genomic_DNA.
DR EMBL; M18276; AAA24551.1; -; Genomic_DNA.
DR PIR; JT0500; BVECRD.
DR RefSeq; NP_415167.1; NC_000913.3.
DR RefSeq; WP_000131719.1; NZ_STEB01000031.1.
DR AlphaFoldDB; P0ABG7; -.
DR SMR; P0ABG7; -.
DR BioGRID; 4259910; 288.
DR ComplexPortal; CPX-5718; Elongasome complex.
DR DIP; DIP-48062N; -.
DR IntAct; P0ABG7; 2.
DR STRING; 511145.b0634; -.
DR TCDB; 2.A.103.1.2; the bacterial murein precursor exporter (mpe) family.
DR PaxDb; P0ABG7; -.
DR PRIDE; P0ABG7; -.
DR EnsemblBacteria; AAC73735; AAC73735; b0634.
DR EnsemblBacteria; BAA35277; BAA35277; BAA35277.
DR GeneID; 58462997; -.
DR GeneID; 945238; -.
DR KEGG; ecj:JW0629; -.
DR KEGG; eco:b0634; -.
DR PATRIC; fig|1411691.4.peg.1634; -.
DR EchoBASE; EB0602; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_2_2_6; -.
DR InParanoid; P0ABG7; -.
DR OMA; IFCTVGE; -.
DR PhylomeDB; P0ABG7; -.
DR BioCyc; EcoCyc:EG10607-MON; -.
DR BioCyc; MetaCyc:EG10607-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P0ABG7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0005886; C:plasma membrane; IDA:EcoCyc.
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; IC:ComplexPortal.
DR GO; GO:0008360; P:regulation of cell shape; IMP:EcoliWiki.
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 1: Evidence at protein level;
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..370
FT /note="Peptidoglycan glycosyltransferase MrdB"
FT /id="PRO_0000062715"
FT TOPO_DOM 1..19
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..74
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..159
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..262
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..335
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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
