RODA_BACSU
ID RODA_BACSU Reviewed; 393 AA.
AC P39604;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Peptidoglycan glycosyltransferase RodA {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000303|PubMed:27525505};
DE Short=PGT {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000303|PubMed:27525505};
DE EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000269|PubMed:27525505};
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:0000303|PubMed:27525505};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000303|PubMed:27525505};
DE Short=PG polymerase {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000305};
DE AltName: Full=Rod shape-determining protein {ECO:0000305};
GN Name=rodA {ECO:0000255|HAMAP-Rule:MF_02079}; Synonyms=ywcF;
GN OrderedLocusNames=BSU38120; ORFNames=ipa-42d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION IN CELL SHAPE, AND NOMENCLATURE.
RX PubMed=9622350; DOI=10.1046/j.1365-2958.1998.00766.x;
RA Henriques A.O., Glaser P., Piggot P.J., Moran C.P. Jr.;
RT "Control of cell shape and elongation by the rodA gene in Bacillus
RT subtilis.";
RL Mol. Microbiol. 28:235-247(1998).
RN [4]
RP FUNCTION AS A GLYCOSYLTRANSFERASE, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR
RP LOCATION, INDUCTION, AND MUTAGENESIS OF TRP-105 AND ASP-280.
RC STRAIN=168 / PY79;
RX PubMed=27525505; DOI=10.1038/nature19331;
RA Meeske A.J., Riley E.P., Robins W.P., Uehara T., Mekalanos J.J., Kahne D.,
RA Walker S., Kruse A.C., Bernhardt T.G., Rudner D.Z.;
RT "SEDS proteins are a widespread family of bacterial cell wall
RT polymerases.";
RL Nature 537:634-638(2016).
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell wall
CC elongation (PubMed:9622350, PubMed:27525505). Also required for the
CC maintenance of the rod cell shape (PubMed:9622350).
CC {ECO:0000269|PubMed:27525505, ECO:0000269|PubMed:9622350}.
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:27525505};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000269|PubMed:27525505}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02079,
CC ECO:0000269|PubMed:27525505}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02079}.
CC -!- INDUCTION: Induced by the ECF sigma factor SigM.
CC {ECO:0000269|PubMed:27525505}.
CC -!- MISCELLANEOUS: Increased expression mediated by SigM is both necessary
CC and sufficient to confer intrinsic resistance to moenomycin and
CC viability to cells lacking aPBPs. {ECO:0000269|PubMed:27525505}.
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; X73124; CAA51598.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15838.1; -; Genomic_DNA.
DR PIR; S39697; S39697.
DR RefSeq; NP_391691.1; NC_000964.3.
DR RefSeq; WP_003227413.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39604; -.
DR SMR; P39604; -.
DR STRING; 224308.BSU38120; -.
DR PaxDb; P39604; -.
DR PRIDE; P39604; -.
DR EnsemblBacteria; CAB15838; CAB15838; BSU_38120.
DR GeneID; 937294; -.
DR KEGG; bsu:BSU38120; -.
DR PATRIC; fig|224308.179.peg.4126; -.
DR eggNOG; COG0772; Bacteria.
DR InParanoid; P39604; -.
DR OMA; PYYQGDL; -.
DR PhylomeDB; P39604; -.
DR BioCyc; BSUB:BSU38120-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Membrane; Peptidoglycan synthesis; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..393
FT /note="Peptidoglycan glycosyltransferase RodA"
FT /id="PRO_0000062724"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02079"
FT MUTAGEN 105
FT /note="W->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:27525505"
FT MUTAGEN 280
FT /note="D->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:27525505"
SQ SEQUENCE 393 AA; 43274 MW; D84864CD368240FB CRC64;
MSRYKKQQSP FYQGDLIFIF GVFFIISVVS IYAAGQFGQY GNTDWIQQIV FYLLGAVAIT
VLLYFDLEQL EKLSLYIFII GILSLIILKI SPESIAPVIK GAKSWFRIGR ITIQPSEFMK
VGLIMMLASV IGKANPKGVR TLRDDIHLLL KIAGVAVIPV GLILMQDAGT AGICMFIVLV
MVFMSGINWK LIAIIAGSGI LLISLILLVM INFPDVAKSV GIQDYQIKRV TSWVSASNET
QEDSNDSWQV DQAIMAIGSG GILGNGISNL KVYVPESTTD FIFSIIGESF GFIGCAIVVI
MFFFLIYRLV VLIDKIHPFN RFASFFCVGY TALIVIHTFQ NIGMNIGIMP VTGIPLLFVS
YGGSSTLSTL IGFGIVYNAS VQLTKYRSYL FNS
