RS1_MYCTU
ID RS1_MYCTU Reviewed; 481 AA.
AC P9WH43; L0TA09; O06147;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=30S ribosomal protein S1;
GN Name=rpsA; OrderedLocusNames=Rv1630; ORFNames=MTCY01B2.22;
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 [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 [2]
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 [3]
RP FUNCTION, TMRNA-BINDING, AND MUTAGENESIS OF ALA-438.
RC STRAIN=H37Rv;
RX PubMed=21835980; DOI=10.1126/science.1208813;
RA Shi W., Zhang X., Jiang X., Yuan H., Lee J.S., Barry C.E. III, Wang H.,
RA Zhang W., Zhang Y.;
RT "Pyrazinamide inhibits trans-translation in Mycobacterium tuberculosis.";
RL Science 333:1630-1632(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 285-438 OF APOPROTEIN AND IN
RP COMPLEX WITH POA, DOMAIN, TMRNA-BINDING, AND MUTAGENESIS OF LYS-303;
RP PHE-307; 307-PHE--PHE-310; PHE-310; ARG-357 AND ALA-438.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=25430994; DOI=10.1111/mmi.12892;
RA Yang J., Liu Y., Bi J., Cai Q., Liao X., Li W., Guo C., Zhang Q., Lin T.,
RA Zhao Y., Wang H., Liu J., Zhang X., Lin D.;
RT "Structural basis for targeting the ribosomal protein S1 of Mycobacterium
RT tuberculosis by pyrazinamide.";
RL Mol. Microbiol. 95:791-803(2015).
CC -!- FUNCTION: Binds mRNA, facilitating recognition of most mRNAs by the 30S
CC ribosomal subunit during translation initiation (By similarity).
CC Probably plays a role in trans-translation; binds tmRNA (the product of
CC the ssrA gene) (PubMed:21835980). In trans-translation Ala-
CC aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA gene;
CC the 2 termini fold to resemble tRNA(Ala) while it encodes a short
CC internal open reading frame (the tag peptide)) acts like a tRNA,
CC entering the A-site of the ribosome and displacing the stalled mRNA
CC (which is subsequently degraded). The ribosome then switches to
CC translate the ORF on the tmRNA, the nascent peptide is terminated with
CC the 'tag peptide' encoded by the tmRNA and thus targeted for
CC degradation (By similarity). {ECO:0000250|UniProtKB:P0AG67,
CC ECO:0000269|PubMed:21835980}.
CC -!- FUNCTION: Binds pyrazinoic acid (POA), the active form of the prodrug
CC pyrazinamide (PZA); POA disrupts tmRNA binding (at 50 ug/ml in vitro)
CC and also trans-translation (at 25 ug/ml in vitro using purified H37Ra
CC ribosomes). {ECO:0000269|PubMed:21835980}.
CC -!- DOMAIN: Full-length S1 protein and the C-terminal domain (residues 285-
CC 481) bind tmRNA; the interaction is disrupted in a concentration-
CC dependent manner by POA. 2 POA molecules bind to the C-terminal domain
CC (residues 285-481) and S1 motif 4 (residues 285-368).
CC {ECO:0000305|PubMed:25430994}.
CC -!- MISCELLANEOUS: Mutations in this gene that alter POA binding may cause
CC antibiotic resistance. {ECO:0000305|PubMed:21835980}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44394.1; -; Genomic_DNA.
DR PIR; D70559; D70559.
DR RefSeq; NP_216146.1; NC_000962.3.
DR RefSeq; WP_003408066.1; NZ_NVQJ01000016.1.
DR PDB; 4NNG; X-ray; 2.02 A; A=285-435.
DR PDB; 4NNI; X-ray; 2.64 A; A/B=285-438.
DR PDB; 4NNK; X-ray; 2.31 A; A=285-434.
DR PDBsum; 4NNG; -.
DR PDBsum; 4NNI; -.
DR PDBsum; 4NNK; -.
DR AlphaFoldDB; P9WH43; -.
DR SMR; P9WH43; -.
DR STRING; 83332.Rv1630; -.
DR PaxDb; P9WH43; -.
DR DNASU; 885188; -.
DR GeneID; 885188; -.
DR KEGG; mtu:Rv1630; -.
DR TubercuList; Rv1630; -.
DR eggNOG; COG0539; Bacteria.
DR OMA; WQQFART; -.
DR PhylomeDB; P9WH43; -.
DR PRO; PR:P9WH43; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR10724:SF7; PTHR10724:SF7; 1.
DR Pfam; PF00575; S1; 4.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 4.
DR SUPFAM; SSF50249; SSF50249; 4.
DR PROSITE; PS50126; S1; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding.
FT CHAIN 1..481
FT /note="30S ribosomal protein S1"
FT /id="PRO_0000196042"
FT DOMAIN 36..105
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 123..188
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 209..277
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 294..363
FT /note="S1 motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 429..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 303
FT /note="K->A: 2.5-fold decrease in binding of POA, decreased
FT binding of tmRNA (expressed as residues 285-481)."
FT /evidence="ECO:0000269|PubMed:25430994"
FT MUTAGEN 307..310
FT /note="FGAF->AGAL: Complete loss of POA binding,
FT significantly decreased binding of tmRNA (expressed as
FT residues 285-481)."
FT /evidence="ECO:0000269|PubMed:25430994"
FT MUTAGEN 307
FT /note="F->A: 2.5-fold decrease in binding of POA, decreased
FT binding of tmRNA (expressed as residues 285-481)."
FT /evidence="ECO:0000269|PubMed:25430994"
FT MUTAGEN 310
FT /note="F->G: 3-fold decrease in binding of POA, decreased
FT binding of tmRNA (expressed as residues 285-481)."
FT /evidence="ECO:0000269|PubMed:25430994"
FT MUTAGEN 357
FT /note="R->A: 2.7-fold decrease in binding of POA, decreased
FT binding of tmRNA (expressed as residues 285-481)."
FT /evidence="ECO:0000269|PubMed:25430994"
FT MUTAGEN 438
FT /note="Missing: Does not bind POA. Binds tmRNA less
FT strongly than wild-type, binding is not disrupted by POA."
FT /evidence="ECO:0000269|PubMed:21835980,
FT ECO:0000269|PubMed:25430994"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:4NNG"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:4NNG"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:4NNG"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:4NNG"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4NNG"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:4NNG"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:4NNG"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:4NNG"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:4NNG"
FT HELIX 362..368
FT /evidence="ECO:0007829|PDB:4NNG"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:4NNG"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:4NNG"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:4NNG"
FT HELIX 408..433
FT /evidence="ECO:0007829|PDB:4NNG"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:4NNI"
SQ SEQUENCE 481 AA; 53202 MW; FD73D8A5D051DBE1 CRC64;
MPSPTVTSPQ VAVNDIGSSE DFLAAIDKTI KYFNDGDIVE GTIVKVDRDE VLLDIGYKTE
GVIPARELSI KHDVDPNEVV SVGDEVEALV LTKEDKEGRL ILSKKRAQYE RAWGTIEALK
EKDEAVKGTV IEVVKGGLIL DIGLRGFLPA SLVEMRRVRD LQPYIGKEIE AKIIELDKNR
NNVVLSRRAW LEQTQSEVRS EFLNNLQKGT IRKGVVSSIV NFGAFVDLGG VDGLVHVSEL
SWKHIDHPSE VVQVGDEVTV EVLDVDMDRE RVSLSLKATQ EDPWRHFART HAIGQIVPGK
VTKLVPFGAF VRVEEGIEGL VHISELAERH VEVPDQVVAV GDDAMVKVID IDLERRRISL
SLKQANEDYT EEFDPAKYGM ADSYDEQGNY IFPEGFDAET NEWLEGFEKQ RAEWEARYAE
AERRHKMHTA QMEKFAAAEA AGRGADDQSS ASSAPSEKTA GGSLASDAQL AALREKLAGS
A
