RS1_MYCS2
ID RS1_MYCS2 Reviewed; 479 AA.
AC A0QYY6;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=30S ribosomal protein S1;
GN Name=rpsA; OrderedLocusNames=MSMEG_3833, MSMEI_3743; ORFNames=LJ00_19040;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=25657281; DOI=10.1128/genomea.01520-14;
RA Mohan A., Padiadpu J., Baloni P., Chandra N.;
RT "Complete genome sequences of a Mycobacterium smegmatis laboratory strain
RT (MC2 155) and isoniazid-resistant (4XR1/R2) mutant strains.";
RL Genome Announc. 3:E01520-E01520(2015).
RN [5]
RP PROTEIN SEQUENCE OF 32-58; 72-93; 112-127; 135-156; 158-167; 188-208;
RP 290-300; 313-347; 364-377 AND 435-472, INTERACTION WITH PROTEIN
RP MSMEG_2731/MSMEI_2664, AND SUBUNIT.
RX PubMed=22590585; DOI=10.1371/journal.pone.0036666;
RA Yang M., Chen Y., Zhou Y., Wang L., Zhang H., Bi L.J., Zhang X.E.;
RT "MSMEG_2731, an uncharacterized nucleic acid binding protein from
RT Mycobacterium smegmatis, physically interacts with RPS1.";
RL PLoS ONE 7:E36666-E36666(2012).
RN [6]
RP FUNCTION.
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 285-445, DOMAIN, AND
RP TMRNA-BINDING.
RC STRAIN=ATCC 700084 / mc(2)155;
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). Plays
CC a role in trans-translation; binds tmRNA (the product of the ssrA gene)
CC (PubMed:25430994). Binds very poorly to pyrazinoic acid (POA), the
CC active form of the prodrug pyrazinamide (PZA); POA does not disrupt
CC trans-translation in this organism (PubMed:21835980). M.smegmatis is
CC resistant to the antibiotic PZA (PubMed:25430994). In trans-translation
CC Ala-aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA
CC gene; 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. {ECO:0000250|UniProtKB:P0AG67,
CC ECO:0000269|PubMed:21835980, ECO:0000269|PubMed:25430994}.
CC -!- SUBUNIT: Binds uncharacterized protein MSMEG_2731/MSMEI_2664.
CC {ECO:0000269|PubMed:22590585}.
CC -!- DOMAIN: Full-length S1 protein and the C-terminal domain (residues 285-
CC 479) bind tmRNA, the interaction is not disrupted by POA. Unlike
CC M.tuberculosis (strain H37Rv) the S1 motif 4 does not bind POA, which
CC may explain why M.smegmatis is resistant to the antibiotic PZA, the
CC precursor to POA. {ECO:0000269|PubMed:25430994}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK74996.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40201.1; -; Genomic_DNA.
DR EMBL; CP009494; AIU08951.1; -; Genomic_DNA.
DR RefSeq; WP_003895279.1; NZ_SIJM01000005.1.
DR RefSeq; YP_888124.1; NC_008596.1.
DR PDB; 4NNH; X-ray; 2.30 A; A/B=285-445.
DR PDBsum; 4NNH; -.
DR AlphaFoldDB; A0QYY6; -.
DR SMR; A0QYY6; -.
DR STRING; 246196.MSMEI_3743; -.
DR PRIDE; A0QYY6; -.
DR EnsemblBacteria; ABK74996; ABK74996; MSMEG_3833.
DR EnsemblBacteria; AFP40201; AFP40201; MSMEI_3743.
DR GeneID; 66735201; -.
DR KEGG; msb:LJ00_19040; -.
DR KEGG; msg:MSMEI_3743; -.
DR KEGG; msm:MSMEG_3833; -.
DR PATRIC; fig|246196.19.peg.3771; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_4_1_11; -.
DR OMA; WQQFART; -.
DR OrthoDB; 1235756at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; Direct protein sequencing; Nucleotidyltransferase;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW Transferase.
FT CHAIN 1..479
FT /note="30S ribosomal protein S1"
FT /id="PRO_0000433568"
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..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:4NNH"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:4NNH"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:4NNH"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:4NNH"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4NNH"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:4NNH"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:4NNH"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:4NNH"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:4NNH"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:4NNH"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:4NNH"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:4NNH"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:4NNH"
FT HELIX 408..443
FT /evidence="ECO:0007829|PDB:4NNH"
SQ SEQUENCE 479 AA; 53316 MW; FF38A2F14ECF21CD CRC64;
MPSPSVTSPQ VAVNDIGSAE DFLAAIDKTI KYFNDGDIVE GTIVKVDRDE VLLDIGYKTE
GVIPSRELSI KHDVDPNEVV SVGDEVEALV LTKEDKEGRL ILSKKRAQYE RAWGTIEELK
EKDEAVKGTV IEVVKGGLIL DIGLRGFLPA SLVEMRRVRD LQPYIGKEIE AKIIELDKNR
NNVVLSRRAW LEQTQSEVRS EFLNQLQKGA IRKGVVSSIV NFGAFVDLGG VDGLVHVSEL
SWKHIDHPSE VVQVGDEVTV EVLDVDMDRE RVSLSLKATQ EDPWRHFART HAIGQIVPGK
VTKLVPFGAF VRVEEGIEGL VHISELSERH VEVPDQVVQV GDDAMVKVID IDLERRRISL
SLKQANEDYT EEFDPSKYGM ADSYDEQGNY IFPEGFDPET NEWLEGFDKQ REEWEARYAE
AERRHKMHTA QMEKFAAAEA EAANAPVSNG SSRSEESSGG TLASDAQLAA LREKLAGNA
