SLTSR_BACSU
ID SLTSR_BACSU Reviewed; 158 AA.
AC O34321;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Salt stress-responsive protein YocM {ECO:0000305};
GN Name=yocM; OrderedLocusNames=BSU19260;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT terC and odhAB loci cloned in a yeast artificial chromosome.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30431188; DOI=10.1111/mmi.14164;
RA Hantke I., Schaefer H., Janczikowski A., Turgay K.;
RT "YocM a small heat shock protein can protect Bacillus subtilis cells during
RT salt stress.";
RL Mol. Microbiol. 111:423-440(2019).
CC -!- FUNCTION: Part of the cellular protein quality control system with a
CC specific role in salt stress response. May facilitate protein
CC homeostasis, together with chemical chaperones that accumulate during
CC the salt stress response. Increased levels of YocM protects against
CC both heat and salt stress. In vitro, displays an unusual aggregase
CC chaperone activity. {ECO:0000269|PubMed:30431188}.
CC -!- SUBUNIT: Forms homodimers, homotetramers and higher oligomers.
CC {ECO:0000269|PubMed:30431188}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Localizes to
CC stress-induced intracellular protein aggregates.
CC {ECO:0000269|PubMed:30431188}.
CC -!- INDUCTION: Induced upon salt stress conditions.
CC {ECO:0000269|PubMed:30431188}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene increases sensitivity toward
CC salt stress. {ECO:0000269|PubMed:30431188}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; AF027868; AAB84479.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13818.1; -; Genomic_DNA.
DR PIR; B69902; B69902.
DR RefSeq; NP_389808.1; NC_000964.3.
DR RefSeq; WP_003231255.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34321; -.
DR SMR; O34321; -.
DR STRING; 224308.BSU19260; -.
DR PaxDb; O34321; -.
DR EnsemblBacteria; CAB13818; CAB13818; BSU_19260.
DR GeneID; 939587; -.
DR KEGG; bsu:BSU19260; -.
DR PATRIC; fig|224308.179.peg.2107; -.
DR eggNOG; COG0071; Bacteria.
DR InParanoid; O34321; -.
DR OMA; KMKQWME; -.
DR PhylomeDB; O34321; -.
DR BioCyc; BSUB:BSU19260-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..158
FT /note="Salt stress-responsive protein YocM"
FT /id="PRO_0000126049"
FT DOMAIN 51..158
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ SEQUENCE 158 AA; 18483 MW; B057E92D94A0BA0C CRC64;
MDFEKMKQWM EFAQQMYGGD FWKQVFDEDQ KTPFMTNGQS PFPFAQQDQR GKGDASFPSM
DIVDTVAEVQ FLIYLPGYRK QDVHILSYGD YLVVKGQRFS YFNEQDFRQK EGKYGSFEKK
IPLSDHLHGK MNAIFKDGIL YITIQKDEGQ AKTIVIDD
