SSRP_CAUVN
ID SSRP_CAUVN Reviewed; 152 AA.
AC B8H482;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=CCNA_01254;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP TMRNA STRUCTURE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=10884408; DOI=10.1073/pnas.97.14.7778;
RA Keiler K.C., Shapiro L., Williams K.P.;
RT "tmRNAs that encode proteolysis-inducing tags are found in all known
RT bacterial genomes: A two-piece tmRNA functions in Caulobacter.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7778-7783(2000).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=12511504; DOI=10.1128/jb.185.2.573-580.2003;
RA Keiler K.C., Shapiro L.;
RT "TmRNA is required for correct timing of DNA replication in Caulobacter
RT crescentus.";
RL J. Bacteriol. 185:573-580(2003).
RN [4]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND TMRNA-BINDING.
RC STRAIN=NA1000 / CB15N;
RX PubMed=15978085; DOI=10.1111/j.1365-2958.2005.04709.x;
RA Hong S.J., Tran Q.A., Keiler K.C.;
RT "Cell cycle-regulated degradation of tmRNA is controlled by RNase R and
RT SmpB.";
RL Mol. Microbiol. 57:565-575(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=19805312; DOI=10.1073/pnas.0904904106;
RA Russell J.H., Keiler K.C.;
RT "Subcellular localization of a bacterial regulatory RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16405-16409(2009).
CC -!- FUNCTION: Required for rescue of stalled ribosomes mediated by trans-
CC translation (By similarity). Binds to and required for stability of
CC mature tmRNA, which it protects from degradation by RNase R (rnr)
CC (PubMed:12511504). Required for correct localization of tmRNA
CC (PubMed:19805312). In this organism the ssrA gene for tmRNA is
CC circularly permutated and is processed into 2 pieces to function
CC (PubMed:10884408). Binds to transfer-messenger RNA (tmRNA), required
CC for 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 ECO:0000269|PubMed:10884408, ECO:0000269|PubMed:12511504,
CC ECO:0000269|PubMed:15978085, ECO:0000269|PubMed:19805312}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00023,
CC ECO:0000269|PubMed:19805312}. Note=The tmRNA-SmpB complex associates
CC with stalled 70S ribosomes (By similarity). Colocalizes with tmRNA in
CC regularly spaced foci indicative of a helix-like structure: in the
CC absence of tmRNA this protein still localizes correctly. Although RNase
CC R (rnr) localizes in a similar helix-like pattern, the 2 helices are
CC out of phase. {ECO:0000255|HAMAP-Rule:MF_00023,
CC ECO:0000269|PubMed:19805312}.
CC -!- INDUCTION: Fluctuates during the cell cycle, being low in early swarmer
CC cells and rising dramatically during the G1-S transition (when tmRNA
CC accumulates). Decreases during DNA replication in stalked cells to rise
CC again as cell division starts, reflecting the stability of tmRNA at all
CC stages of the cell cycle (at protein level).
CC {ECO:0000269|PubMed:15978085}.
CC -!- DISRUPTION PHENOTYPE: Delays the cell cycle during the G1-to-S
CC transition (same phenotype as an ssrA deletion), a 10-fold decrease in
CC levels of mature tmRNA (PubMed:12511504). tmRNA is incorrectly
CC localized in cells missing this gene (PubMed:19805312).
CC {ECO:0000269|PubMed:12511504, ECO:0000269|PubMed:15978085,
CC ECO:0000269|PubMed:19805312}.
CC -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000255|HAMAP-
CC Rule:MF_00023}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001340; ACL94719.1; -; Genomic_DNA.
DR RefSeq; WP_010919079.1; NC_011916.1.
DR RefSeq; YP_002516627.1; NC_011916.1.
DR AlphaFoldDB; B8H482; -.
DR SMR; B8H482; -.
DR PRIDE; B8H482; -.
DR EnsemblBacteria; ACL94719; ACL94719; CCNA_01254.
DR GeneID; 7332983; -.
DR KEGG; ccs:CCNA_01254; -.
DR PATRIC; fig|565050.3.peg.1236; -.
DR HOGENOM; CLU_108953_0_1_5; -.
DR OMA; WTNHSAR; -.
DR OrthoDB; 1720952at2; -.
DR PhylomeDB; B8H482; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0070929; P:trans-translation; IEA:UniProtKB-UniRule.
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 Cell cycle; Cytoplasm; Reference proteome; RNA-binding.
FT CHAIN 1..152
FT /note="SsrA-binding protein"
FT /id="PRO_1000197612"
FT REGION 124..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 152 AA; 17545 MW; 3DDC377D68CABEBB CRC64;
MSKPIAENRR ARFDYFIEET FEAGIMLTGT EVKSLRTGRA NIAESYASVE GREIVLINAD
IPPYGHANRF NHEPRRHRKL LLHRRQIDKL IGAVQREGRT LVPIKLYWND KGLAKLEVGL
AKGKKLHDKR DTAAERDWQR DKARLMKGDR GD
