WAG31_MYCS2
ID WAG31_MYCS2 Reviewed; 272 AA.
AC A0R006;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Cell wall synthesis protein Wag31;
DE AltName: Full=Antigen 84;
GN Name=wag31; Synonyms=ag84; OrderedLocusNames=MSMEG_4217, MSMEI_4119;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18310019; DOI=10.1099/mic.0.2007/014076-0;
RA Kang C.M., Nyayapathy S., Lee J.Y., Suh J.W., Husson R.N.;
RT "Wag31, a homologue of the cell division protein DivIVA, regulates growth,
RT morphology and polar cell wall synthesis in mycobacteria.";
RL Microbiology 154:725-735(2008).
RN [5]
RP FUNCTION, AND INTERACTION WITH PBPB.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=19496931; DOI=10.1111/j.1365-2958.2009.06750.x;
RA Mukherjee P., Sureka K., Datta P., Hossain T., Barik S., Das K.P.,
RA Kundu M., Basu J.;
RT "Novel role of Wag31 in protection of mycobacteria under oxidative
RT stress.";
RL Mol. Microbiol. 73:103-119(2009).
RN [6]
RP INDUCTION.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=21470298; DOI=10.1111/j.1574-6968.2011.02278.x;
RA Dahl J.L., Lau Bonilla D.;
RT "The wag31 gene of Mycobacterium tuberculosis is positively regulated by
RT the stringent response.";
RL FEMS Microbiol. Lett. 319:153-159(2011).
RN [7]
RP INTERACTION WITH CWSA.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=23002219; DOI=10.1128/jb.01005-12;
RA Plocinski P., Arora N., Sarva K., Blaszczyk E., Qin H., Das N.,
RA Plocinska R., Ziolkiewicz M., Dziadek J., Kiran M., Gorla P., Cross T.A.,
RA Madiraju M., Rajagopalan M.;
RT "Mycobacterium tuberculosis CwsA interacts with CrgA and Wag31, and the
RT CrgA-CwsA complex is involved in peptidoglycan synthesis and cell shape
RT determination.";
RL J. Bacteriol. 194:6398-6409(2012).
CC -!- FUNCTION: Important for maintaining cell shape and cell wall integrity
CC by localizing peptidoglycan synthesis to the cell poles. Protects PbpB
CC (PBP3, FtsI) from oxidative stress-induced cleavage.
CC {ECO:0000269|PubMed:18310019, ECO:0000269|PubMed:19496931}.
CC -!- SUBUNIT: Forms homooligomers (By similarity). Interacts with PbpB and
CC CwsA. {ECO:0000250, ECO:0000269|PubMed:19496931,
CC ECO:0000269|PubMed:23002219}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18310019}.
CC Note=Localizes to the cell poles.
CC -!- INDUCTION: Positively regulated by the stringent response.
CC {ECO:0000269|PubMed:21470298}.
CC -!- PTM: Phosphorylated by PknA. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Depletion causes a morphological change in which
CC one end of the cell becomes round rather than rod-shaped. This
CC phenotype is caused by the absence or dispersal of peptidoglycan
CC synthesis. {ECO:0000269|PubMed:18310019}.
CC -!- SIMILARITY: Belongs to the DivIVA family. {ECO:0000305}.
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DR EMBL; CP000480; ABK72820.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40576.1; -; Genomic_DNA.
DR RefSeq; WP_011729650.1; NZ_SIJM01000003.1.
DR RefSeq; YP_888494.1; NC_008596.1.
DR AlphaFoldDB; A0R006; -.
DR SMR; A0R006; -.
DR STRING; 246196.MSMEI_4119; -.
DR PRIDE; A0R006; -.
DR EnsemblBacteria; ABK72820; ABK72820; MSMEG_4217.
DR EnsemblBacteria; AFP40576; AFP40576; MSMEI_4119.
DR GeneID; 66735564; -.
DR KEGG; msg:MSMEI_4119; -.
DR KEGG; msm:MSMEG_4217; -.
DR PATRIC; fig|246196.19.peg.4138; -.
DR eggNOG; COG3599; Bacteria.
DR OMA; VNKRFQP; -.
DR OrthoDB; 875822at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell shape; Coiled coil; Cytoplasm;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..272
FT /note="Cell wall synthesis protein Wag31"
FT /id="PRO_0000421156"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 30..67
FT /evidence="ECO:0000255"
FT COILED 139..206
FT /evidence="ECO:0000255"
FT COMPBIAS 81..98
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 272 AA; 29544 MW; 3A6AFB2E22610461 CRC64;
MPLTPADVHN VAFSKPPIGK RGYNEDEVDA FLDLVENELT RLIEENADLR QRVAELDQEL
AAARSGAGAS SQATSSIPLY EPEPEPAPAP PQPVYEAPAQ PAAPQSEDTA VRAARVLSLA
QDTADRLTST AKAEADKLLS DARAQAEAMV SDARQTAETT VSEARQRADA MLADAQTRSE
AQLRQAQEKA DALQADAERK HSEIMGTINQ QRTVLEGRLE QLRTFEREYR TRLKTYLESQ
LEELGQRGSA APVDSSANSD ASGFGQFNRG NN
