RODA_MYCTU
ID RODA_MYCTU Reviewed; 469 AA.
AC P9WN99; L0T251; P63760; P71587;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Peptidoglycan glycosyltransferase RodA {ECO:0000305};
DE EC=2.4.1.129 {ECO:0000305|PubMed:29530985};
DE AltName: Full=Non-canonical transglycosylase RodA {ECO:0000303|PubMed:29530985};
GN Name=rodA {ECO:0000303|PubMed:29530985}; OrderedLocusNames=Rv0017c;
GN ORFNames=MTCY10H4.17c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, PHOSPHORYLATION
RP AT THR-463, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-463.
RX PubMed=29530985; DOI=10.1074/jbc.m117.811190;
RA Arora D., Chawla Y., Malakar B., Singh A., Nandicoori V.K.;
RT "The transpeptidase PbpA and noncanonical transglycosylase RodA of
RT Mycobacterium tuberculosis play important roles in regulating bacterial
RT cell lengths.";
RL J. Biol. Chem. 293:6497-6516(2018).
CC -!- FUNCTION: Transglycosylase involved in peptidoglycan cell wall
CC formation (PubMed:29530985). Required for the regulation of cell
CC length. Plays critical roles for the survival of the pathogen inside
CC the host. Required for both bacterial survival and formation of
CC granuloma structures in a guinea pig infection model (PubMed:29530985).
CC {ECO:0000269|PubMed:29530985}.
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;
CC Evidence={ECO:0000305|PubMed:29530985};
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-463 may be important for
CC modulating interactions with other cell division proteins, thus
CC regulating the cell division process. {ECO:0000269|PubMed:29530985}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000305|PubMed:29530985}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- PTM: Phosphorylated on Thr-463, probably by PknB and PknH.
CC {ECO:0000269|PubMed:29530985}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene does not impact in vitro
CC growth, but it leads to aberrations in the cell length. Deletion
CC enhances sensitivity to nisin and vancomycin. Also exhibits
CC hypersensitivity to moenomycin. Mutant shows compromised bacterial
CC virulence in the host. {ECO:0000269|PubMed:29530985}.
CC -!- SIMILARITY: Belongs to the SEDS family. {ECO:0000305}.
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DR EMBL; AL123456; CCP42739.1; -; Genomic_DNA.
DR PIR; G70699; G70699.
DR RefSeq; NP_214531.1; NC_000962.3.
DR RefSeq; WP_003400364.1; NZ_NVQJ01000005.1.
DR AlphaFoldDB; P9WN99; -.
DR SMR; P9WN99; -.
DR STRING; 83332.Rv0017c; -.
DR PaxDb; P9WN99; -.
DR DNASU; 887075; -.
DR GeneID; 887075; -.
DR KEGG; mtu:Rv0017c; -.
DR TubercuList; Rv0017c; -.
DR eggNOG; COG0772; Bacteria.
DR OMA; IFCTVGE; -.
DR PhylomeDB; P9WN99; -.
DR UniPathway; UPA00219; -.
DR PHI-base; PHI:7982; -.
DR Proteomes; UP000001584; 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-EC.
DR GO; GO:0051301; P:cell division; IDA:MTBBASE.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0052559; P:induction by symbiont of host immune response; IDA:MTBBASE.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR InterPro; IPR001182; FtsW/RodA.
DR PANTHER; PTHR30474; PTHR30474; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 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; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..469
FT /note="Peptidoglycan glycosyltransferase RodA"
FT /id="PRO_0000062710"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29530985"
FT MUTAGEN 463
FT /note="T->A: Can rescue the moenomycin sensitivity
FT phenotype of the deletion mutant, but cannot rescue the
FT aberrant short-length phenotype."
FT /evidence="ECO:0000269|PubMed:29530985"
FT MUTAGEN 463
FT /note="T->E: Can rescue the moenomycin sensitivity
FT phenotype and the aberrant short-length phenotype of the
FT deletion mutant."
FT /evidence="ECO:0000269|PubMed:29530985"
SQ SEQUENCE 469 AA; 50611 MW; F4DBB2AB46ED72BA CRC64;
MTTRLQAPVA VTPPLPTRRN AELLLLCFAA VITFAALLVV QANQDQGVPW DLTSYGLAFL
TLFGSAHLAI RRFAPYTDPL LLPVVALLNG LGLVMIHRLD LVDNEIGEHR HPSANQQMLW
TLVGVAAFAL VVTFLKDHRQ LARYGYICGL AGLVFLAVPA LLPAALSEQN GAKIWIRLPG
FSIQPAEFSK ILLLIFFSAV LVAKRGLFTS AGKHLLGMTL PRPRDLAPLL AAWVISVGVM
VFEKDLGASL LLYTSFLVVV YLATQRFSWV VIGLTLFAAG TLVAYFIFEH VRLRVQTWLD
PFADPDGTGY QIVQSLFSFA TGGIFGTGLG NGQPDTVPAA STDFIIAAFG EELGLVGLTA
ILMLYTIVII RGLRTAIATR DSFGKLLAAG LSSTLAIQLF IVVGGVTRLI PLTGLTTPWM
SYGGSSLLAN YILLAILARI SHGARRPLRT RPRNKSPITA AGTEVIERV
