RS1_MYCLE
ID RS1_MYCLE Reviewed; 481 AA.
AC P46836;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=30S ribosomal protein S1;
GN Name=rpsA; OrderedLocusNames=ML1382;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7476188; DOI=10.1111/j.1365-2958.1995.tb02317.x;
RA Fsihi H., Cole S.T.;
RT "The Mycobacterium leprae genome: systematic sequence analysis identifies
RT key catabolic enzymes, ATP-dependent transport systems and a novel polA
RT locus associated with genomic variability.";
RL Mol. Microbiol. 16:909-919(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Binds mRNA; thus facilitating recognition of the initiation
CC point. It is needed to translate mRNA with a short Shine-Dalgarno (SD)
CC purine-rich sequence (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000305}.
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DR EMBL; Z46257; CAA86365.1; -; Genomic_DNA.
DR EMBL; AL583921; CAC31763.1; -; Genomic_DNA.
DR PIR; H87081; H87081.
DR PIR; S77660; S77660.
DR RefSeq; NP_301983.1; NC_002677.1.
DR RefSeq; WP_010908304.1; NC_002677.1.
DR PDB; 5IE8; NMR; -; A=280-368.
DR PDBsum; 5IE8; -.
DR AlphaFoldDB; P46836; -.
DR BMRB; P46836; -.
DR SMR; P46836; -.
DR STRING; 272631.ML1382; -.
DR PRIDE; P46836; -.
DR EnsemblBacteria; CAC31763; CAC31763; CAC31763.
DR KEGG; mle:ML1382; -.
DR PATRIC; fig|272631.5.peg.2565; -.
DR Leproma; ML1382; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_4_1_11; -.
DR OMA; WQQFART; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005840; C:ribosome; 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; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding.
FT CHAIN 1..481
FT /note="30S ribosomal protein S1"
FT /id="PRO_0000196041"
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 437..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 224..228
FT /note="AFVDL -> CVCRS (in Ref. 1; CAA86365)"
FT /evidence="ECO:0000305"
FT CONFLICT 364..393
FT /note="QANEDYIEEFDPAKYGMADSYDEQGNYIFP -> ADQRGLHRGVRPGKVRYG
FT PTATTSRATTSSL (in Ref. 1; CAA86365)"
FT /evidence="ECO:0000305"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:5IE8"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:5IE8"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:5IE8"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:5IE8"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:5IE8"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:5IE8"
FT STRAND 342..352
FT /evidence="ECO:0007829|PDB:5IE8"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:5IE8"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:5IE8"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:5IE8"
SQ SEQUENCE 481 AA; 53279 MW; 4F955F6D8EA8E09B CRC64;
MSIPAVPSPQ IAVNDVGSSE DFLAAIDKTI KYFNDGDIVE GTIVKVDRDE VLLDIGYKTE
GVIPARELSI KHDVDPNEVV SVGDEVEALV LTKEDKEGRL ILSKKRAQYE RAWGTIEALK
EKDEAVKGIV IEVVKGGLIL DIGLRGFLPA SLVEMRRVRD LQPYIGKEIE AKIIELDKNR
NNVVLSRRAW LEQTQSEVRS EFLNQLQKGA IRKGVVSSIV NFGAFVDLGG VDGLVHVSEL
SWKHIDHPSE VVQVGNEVTV EVLDVDMDRE RVSLSLKATQ EDPWRHFART HAIGQIVPGK
VTKLVPFGAF VRVEEGIEGL VHISELAERH VEVPDQVVAV GDDAMVKVID IDLERRRISL
SLKQANEDYI EEFDPAKYGM ADSYDEQGNY IFPEGFDPDS NEWLEGFDTQ RAEWEARYAE
AERRYKMHTI QMEKFAATEE AGHGSSEQPP ASSTPSAKAT GGSLASDAQL AALREKLAGS
A
