RODA_MYCLE
ID RODA_MYCLE Reviewed; 465 AA.
AC Q50186;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Peptidoglycan glycosyltransferase RodA {ECO:0000250|UniProtKB:P9WN99};
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P9WN99};
DE AltName: Full=Non-canonical transglycosylase RodA {ECO:0000250|UniProtKB:P9WN99};
GN Name=rodA; OrderedLocusNames=ML0019;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fsihi H., Salazar L., Takiff H.E., Cole S.T.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Transglycosylase involved in peptidoglycan cell wall
CC formation. Required for the regulation of cell length.
CC {ECO:0000250|UniProtKB:P9WN99}.
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:0000250|UniProtKB:P9WN99};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000250|UniProtKB:P9WN99}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P9WN99}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SEDS family. {ECO:0000305}.
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DR EMBL; Z70722; CAA94715.1; -; Genomic_DNA.
DR EMBL; AL583917; CAC29527.1; -; Genomic_DNA.
DR PIR; C86911; C86911.
DR PIR; T10012; T10012.
DR RefSeq; NP_301145.1; NC_002677.1.
DR RefSeq; WP_010907470.1; NC_002677.1.
DR AlphaFoldDB; Q50186; -.
DR SMR; Q50186; -.
DR STRING; 272631.ML0019; -.
DR EnsemblBacteria; CAC29527; CAC29527; CAC29527.
DR KEGG; mle:ML0019; -.
DR PATRIC; fig|272631.5.peg.23; -.
DR Leproma; ML0019; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_3_1_11; -.
DR OMA; IFCTVGE; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 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..465
FT /note="Peptidoglycan glycosyltransferase RodA"
FT /id="PRO_0000062709"
FT TRANSMEM 21..41
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 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 319..320
FT /note="GI -> VY (in Ref. 1; CAA94715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 50469 MW; CA656039538EBC24 CRC64;
MTTQLQPVVT VTPPLPTRRN AELLLLGFAA VITVAALAIV EANQERNFRW YLAGYGLIFW
SLFASAHLAI RRFAPYTDPL LLPIVALLNG LGLVMIHRLD LVDNDVTGHH HTSAAQQMLW
TLVGVAAFVL VMTVLKDHRQ LARYGYISGL TGLVFLAIPA PLPEQNGAKI WIRFPGFSIQ
PAEFSKILLL IFFAAVLVAK RSLFTSAGKH LIGMTLPRPR DLAPLLAAWV ISVSVMVFEK
DLGTSLLLYA SFLVVVYLAT QRLSWVIIGL VLFTAGSTIA YFTFEHIRVR MQVWWDPFTN
LDVGGYQIVQ SLFSFATGGI FGTGLGNGQP DAIPAASTDF IIAVFGEELG LVGLAALLML
YTIVIVRGLR TAIATRDSFG KLLAAGLAST LAIQLFIVSG GVTTLIPLTG LTTPWMSYGG
SSLLANYVLL AILARISHSA RHPLRSRPHN TSPIAVASTE VIERV
