ID   WAG31_MYCTO             Reviewed;         260 AA.
AC   P9WMU0; L0TBN0; P0A5N2; P46816;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Cell wall synthesis protein Wag31;
DE   AltName: Full=Antigen 84;
GN   Name=wag31; Synonyms=ag84; OrderedLocusNames=MT2204;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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. Phosphorylation enhances polar
CC       localization, which in turn heightens polar peptidoglycan biosynthesis
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DivIVA family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46488.1; -; Genomic_DNA.
DR   PIR; E70578; E70578.
DR   RefSeq; WP_003411131.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMU0; -.
DR   SMR; P9WMU0; -.
DR   EnsemblBacteria; AAK46488; AAK46488; MT2204.
DR   KEGG; mtc:MT2204; -.
DR   PATRIC; fig|83331.31.peg.2377; -.
DR   HOGENOM; CLU_062236_0_0_11; -.
DR   Proteomes; UP000001020; 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; Stress response.
FT   CHAIN           1..260
FT                   /note="Cell wall synthesis protein Wag31"
FT                   /id="PRO_0000427243"
FT   REGION          233..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          31..64
FT                   /evidence="ECO:0000255"
FT   COILED          161..196
FT                   /evidence="ECO:0000255"
FT   MOD_RES         73
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   260 AA;  28277 MW;  D36113355149CEDC CRC64;
     MPLTPADVHN VAFSKPPIGK RGYNEDEVDA FLDLVENELT RLIEENSDLR QRINELDQEL
     AAGGGAGVTP QATQAIPAYE PEPGKPAPAA VSAGMNEEQA LKAARVLSLA QDTADRLTNT
     AKAESDKMLA DARANAEQIL GEARHTADAT VAEARQRADA MLADAQSRSE AQLRQAQEKA
     DALQADAERK HSEIMGTINQ QRAVLEGRLE QLRTFEREYR TRLKTYLESQ LEELGQRGSA
     APVDSNADAG GFDQFNRGKN