SSRP_BACSU
ID SSRP_BACSU Reviewed; 156 AA.
AC O32230;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=SsrA-binding protein {ECO:0000255|HAMAP-Rule:MF_00023};
DE AltName: Full=Small protein B {ECO:0000255|HAMAP-Rule:MF_00023};
GN Name=smpB {ECO:0000255|HAMAP-Rule:MF_00023}; Synonyms=yvaI;
GN OrderedLocusNames=BSU33600;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / 1012;
RX PubMed=11395451; DOI=10.1128/jb.183.13.3885-3889.2001;
RA Wiegert T., Schumann W.;
RT "SsrA-mediated tagging in Bacillus subtilis.";
RL J. Bacteriol. 183:3885-3889(2001).
RN [3]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17369301; DOI=10.1128/jb.00062-07;
RA Shin J.H., Price C.W.;
RT "The SsrA-SmpB ribosome rescue system is important for growth of Bacillus
RT subtilis at low and high temperatures.";
RL J. Bacteriol. 189:3729-3737(2007).
RN [4]
RP PROBABLE FUNCTION IN SPORULATION.
RC STRAIN=168;
RX PubMed=18673456; DOI=10.1111/j.1365-2958.2008.06381.x;
RA Abe T., Sakaki K., Fujihara A., Ujiie H., Ushida C., Himeno H., Sato T.,
RA Muto A.;
RT "tmRNA-dependent trans-translation is required for sporulation in Bacillus
RT subtilis.";
RL Mol. Microbiol. 69:1491-1498(2008).
CC -!- FUNCTION: Required for rescue of stalled ribosomes mediated by trans-
CC translation. Binds to transfer-messenger RNA (tmRNA), required for
CC stable association of tmRNA with ribosomes. tmRNA and SmpB together
CC mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is
CC encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and
CC it encodes a 'tag peptide', a short internal open reading frame. During
CC trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering
CC the A-site of stalled ribosomes, displacing the stalled mRNA. The
CC ribosome then switches to translate the ORF on the tmRNA; the nascent
CC peptide is terminated with the 'tag peptide' encoded by the tmRNA and
CC targeted for degradation. The ribosome is freed to recommence
CC translation, which seems to be the essential function of trans-
CC translation (By similarity). Required for trans-translation
CC (PubMed:11395451). Probably required for sporulation; deletion of the
CC gene for tmRNA impairs sporulation via its effect on trans-translation,
CC and as smpB is required for trans-translation under non-stress
CC conditions, it is also probably required during sporulation
CC (PubMed:18673456). {ECO:0000255|HAMAP-Rule:MF_00023,
CC ECO:0000269|PubMed:11395451, ECO:0000305|PubMed:18673456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00023}.
CC Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes.
CC {ECO:0000255|HAMAP-Rule:MF_00023}.
CC -!- INDUCTION: Constitutively expressed, part of a 5 gene operon with
CC multiple promoters. Not ethanol-stress induced.
CC {ECO:0000269|PubMed:17369301}.
CC -!- DISRUPTION PHENOTYPE: Not essential for growth; loss of trans-
CC translation (PubMed:11395451). Significantly decreased growth at 16 and
CC 52 degrees Celsius (PubMed:17369301). {ECO:0000269|PubMed:11395451,
CC ECO:0000269|PubMed:17369301}.
CC -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000255|HAMAP-
CC Rule:MF_00023}.
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DR EMBL; AL009126; CAB15365.1; -; Genomic_DNA.
DR PIR; F70027; F70027.
DR RefSeq; NP_391240.1; NC_000964.3.
DR RefSeq; WP_003220025.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32230; -.
DR SMR; O32230; -.
DR STRING; 224308.BSU33600; -.
DR PaxDb; O32230; -.
DR PRIDE; O32230; -.
DR EnsemblBacteria; CAB15365; CAB15365; BSU_33600.
DR GeneID; 64305121; -.
DR GeneID; 936170; -.
DR KEGG; bsu:BSU33600; -.
DR PATRIC; fig|224308.179.peg.3645; -.
DR eggNOG; COG0691; Bacteria.
DR InParanoid; O32230; -.
DR OMA; WTNHSAR; -.
DR PhylomeDB; O32230; -.
DR BioCyc; BSUB:BSU33600-MON; -.
DR PRO; PR:O32230; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0070929; P:trans-translation; IEA:UniProtKB-UniRule.
DR GO; GO:0070930; P:trans-translation-dependent protein tagging; IMP:UniProtKB.
DR CDD; cd09294; SmpB; 1.
DR Gene3D; 2.40.280.10; -; 1.
DR HAMAP; MF_00023; SmpB; 1.
DR InterPro; IPR023620; SmpB.
DR InterPro; IPR000037; SsrA-bd_prot.
DR InterPro; IPR020081; SsrA-bd_prot_CS.
DR PANTHER; PTHR30308; PTHR30308; 1.
DR Pfam; PF01668; SmpB; 1.
DR SUPFAM; SSF74982; SSF74982; 1.
DR TIGRFAMs; TIGR00086; smpB; 1.
DR PROSITE; PS01317; SSRP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; RNA-binding; Sporulation.
FT CHAIN 1..156
FT /note="SsrA-binding protein"
FT /id="PRO_0000102906"
SQ SEQUENCE 156 AA; 18091 MW; 4487EF725EF200DC CRC64;
MPKGSGKVLS QNKKANHDYF IEETYETGIV LQGTEIKSIR AGRVNLKDSF AKIERGEVFL
HNMHVSPYEQ GNRYNHDPLR TRKLLMHRKE INKLIGLTKE KGYSLVPLKL YLKNGFAKVL
LGLGKGKKNY DKREDLKRKD AKREIERAFR DSQKGF
