WAG31_MYCLE
ID WAG31_MYCLE Reviewed; 266 AA.
AC P46815;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Cell wall synthesis protein Wag31;
DE AltName: Full=Antigen 84;
GN Name=wag31; Synonyms=ag84; OrderedLocusNames=ML0922;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7868268; DOI=10.1128/iai.63.3.954-960.1995;
RA Hermans P.W.M., Abebe F., Kuteyi V.I.O., Kolk A.H.J., Thole J.E.R.,
RA Harboe M.;
RT "Molecular and immunological characterization of the highly conserved
RT antigen 84 from Mycobacterium tuberculosis and Mycobacterium leprae.";
RL Infect. Immun. 63:954-960(1995).
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: Important for maintaining cell shape and cell wall integrity
CC by localizing peptidoglycan synthesis to the cell poles. {ECO:0000250}.
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to the
CC cell poles. {ECO:0000250}.
CC -!- PTM: Phosphorylated by PknA. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DivIVA family. {ECO:0000305}.
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DR EMBL; X77128; CAA54384.1; -; Genomic_DNA.
DR EMBL; AL583920; CAC31303.1; -; Genomic_DNA.
DR PIR; S41931; S41931.
DR RefSeq; NP_301705.1; NC_002677.1.
DR RefSeq; WP_010908029.1; NC_002677.1.
DR AlphaFoldDB; P46815; -.
DR SMR; P46815; -.
DR STRING; 272631.ML0922; -.
DR EnsemblBacteria; CAC31303; CAC31303; CAC31303.
DR KEGG; mle:ML0922; -.
DR PATRIC; fig|272631.5.peg.1665; -.
DR Leproma; ML0922; -.
DR eggNOG; COG3599; Bacteria.
DR HOGENOM; CLU_062236_0_0_11; -.
DR OMA; VNKRFQP; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR019933; DivIVA_domain.
DR InterPro; IPR007793; DivIVA_fam.
DR PANTHER; PTHR35794; PTHR35794; 2.
DR Pfam; PF05103; DivIVA; 1.
DR TIGRFAMs; TIGR03544; DivI1A_domain; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell shape; Coiled coil; Cytoplasm;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..266
FT /note="Cell wall synthesis protein Wag31"
FT /id="PRO_0000064491"
FT REGION 239..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 31..64
FT /evidence="ECO:0000255"
FT COILED 152..203
FT /evidence="ECO:0000255"
FT MOD_RES 77
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 266 AA; 28873 MW; 73675ABB39DA408A CRC64;
MPLTPADVHN VAFSKPPIGK RGYNEDEVDA FLDLVENELT QLIEENSDLR QRIEELDHEL
AAGGGTGAGP VIAVQPTQAL STFEPELVSA KQAPVAAVAE TAEELAMKAT RVLSLAQDTA
DQLTSTAKVE SDKMLADARV NADQILGEAR LTAEATVAEA QQRADAMLAD AQTRSEVQSR
QAQEKADALQ AEAERKHSEI MGAISQQRTV LEGRLEQLRT FEREYRTRLK TYLESQLEEL
GQRGSAAPVD SNADAGGFDQ FNRGNN
