ID   SSRP_MYCTU              Reviewed;         160 AA.
AC   P9WGD3; L0TD60; O05778; P0A612; P96294;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
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}; OrderedLocusNames=Rv3100c;
GN   ORFNames=MTCY164.11c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=8921846; DOI=10.1016/0378-1119(96)00271-5;
RA   Tyagi J.S., Das T.K., Kinger A.K.;
RT   "An M. tuberculosis DNA fragment contains genes encoding cell division
RT   proteins ftsX and ftsE, a basic protein and homologues of PemK and small
RT   protein B.";
RL   Gene 177:59-67(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=H37Rv;
RX   PubMed=24145139; DOI=10.1016/j.tube.2013.09.007;
RA   Personne Y., Parish T.;
RT   "Mycobacterium tuberculosis possesses an unusual tmRNA rescue system.";
RL   Tuberculosis 94:34-42(2014).
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. {ECO:0000255|HAMAP-Rule:MF_00023}.
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   -!- DISRUPTION PHENOTYPE: Not essential for aerobic growth in vitro, has a
CC       20% decrease in tmRNA levels. Increased sensitivity to antibiotics that
CC       inhibit translation (chloramphenicol and erythromycin) but not
CC       transcription (rifampicin). No change in sensitivity to pyrazinamide
CC       (PZA). Unlike smpB, the gene for tmRNA (ssr, 10Sa RNA) is essential.
CC       Strains with ssr or smpB disruptions are not more sensitive to
CC       pyrazinamide, suggesting the prodrug does not directly target either of
CC       these components of trans-translation. {ECO:0000269|PubMed:24145139}.
CC   -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00023}.
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DR   EMBL; X70031; CAA49621.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP45910.1; -; Genomic_DNA.
DR   PIR; C70919; C70919.
DR   RefSeq; NP_217616.1; NC_000962.3.
DR   RefSeq; WP_003416113.1; NZ_NVQJ01000011.1.
DR   AlphaFoldDB; P9WGD3; -.
DR   SMR; P9WGD3; -.
DR   STRING; 83332.Rv3100c; -.
DR   PaxDb; P9WGD3; -.
DR   GeneID; 45427099; -.
DR   GeneID; 888675; -.
DR   KEGG; mtu:Rv3100c; -.
DR   TubercuList; Rv3100c; -.
DR   eggNOG; COG0691; Bacteria.
DR   OMA; WTNHSAR; -.
DR   PhylomeDB; P9WGD3; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0070929; P:trans-translation; IEA:UniProtKB-UniRule.
DR   GO; GO:0070930; P:trans-translation-dependent protein tagging; IBA:GO_Central.
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.
FT   CHAIN           1..160
FT                   /note="SsrA-binding protein"
FT                   /id="PRO_0000102991"
FT   CONFLICT        14
FT                   /note="S -> R (in Ref. 1; CAA49621)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   160 AA;  18230 MW;  949F6327A03ACCD3 CRC64;
     MSKSSRGGRQ IVASNRKARH NYSIIEVFEA GVALQGTEVK SLREGQASLA DSFATIDDGE
     VWLRNAHIPE YRHGSWTNHE PRRNRKLLLH RRQIDTLVGK IREGNFALVP LSLYFAEGKV
     KVELALARGK QARDKRQDMA RRDAQREVLR ELGRRAKGMT