SSRP_NEIMB
ID SSRP_NEIMB Reviewed; 148 AA.
AC P0A0Y8; Q51111;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=NMB1526;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=8852280; DOI=10.1006/mpat.1995.0074;
RA Jennings M.P., Bisercic M., Dunn K.L.R., Martin A., Wilkes K.E., Virji M.,
RA Richards J.C., Moxon E.R.;
RT "Cloning and molecular analysis of the Isi1 (rfaF) gene of Neisseria
RT meningitidis which encodes a heptosyl-2-transferase involved in LPS
RT biosynthesis: evaluation of surface exposed carbohydrates in LPS mediated
RT toxicity for human endothelial cells.";
RL Microb. Pathog. 19:391-407(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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 -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000255|HAMAP-
CC Rule:MF_00023}.
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DR EMBL; U23782; AAC44080.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF41881.1; -; Genomic_DNA.
DR PIR; B81073; B81073.
DR RefSeq; NP_274533.1; NC_003112.2.
DR RefSeq; WP_002229688.1; NC_003112.2.
DR AlphaFoldDB; P0A0Y8; -.
DR SMR; P0A0Y8; -.
DR STRING; 122586.NMB1526; -.
DR PaxDb; P0A0Y8; -.
DR EnsemblBacteria; AAF41881; AAF41881; NMB1526.
DR GeneID; 61281702; -.
DR KEGG; nme:NMB1526; -.
DR PATRIC; fig|122586.8.peg.1935; -.
DR HOGENOM; CLU_108953_3_0_4; -.
DR OMA; WTNHSAR; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Reference proteome; RNA-binding.
FT CHAIN 1..148
FT /note="SsrA-binding protein"
FT /id="PRO_0000102994"
FT REGION 119..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 37..39
FT /note="RVQ -> LSM (in Ref. 1; AAC44080)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="I -> M (in Ref. 1; AAC44080)"
FT /evidence="ECO:0000305"
FT CONFLICT 76..79
FT /note="PRKL -> RASF (in Ref. 1; AAC44080)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="I -> N (in Ref. 1; AAC44080)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="I -> T (in Ref. 1; AAC44080)"
FT /evidence="ECO:0000305"
FT CONFLICT 104..106
FT /note="DLH -> GFA (in Ref. 1; AAC44080)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 17179 MW; B80FDB82161C1D6C CRC64;
MAIANNKKAF HDFFIEDRIE AGLVLEGWEV KAIRAARVQL KESYIYWKKD AFYLVGCHIT
ALPTASTHIK PDAVRPRKLL LNQSEINKLI GKTERAGYTI VPLDLHFSRG KIKMEIGLAK
GKKQHDKRQS MKEADWKREK QRLIKHTR
