RS5_MYCTU
ID RS5_MYCTU Reviewed; 220 AA.
AC P9WH33; L0T4I4; P66574; P95069;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=Rv0721;
GN ORFNames=MTCY210.40;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC -!- FUNCTION: Located at the back of the 30S subunit body where it
CC stabilizes the conformation of the head with respect to the body.
CC {ECO:0000255|HAMAP-Rule:MF_01307}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and
CC S8. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC subunit; the C-terminal domain interacts with the body and contacts
CC protein S4. The interaction surface between S4 and S5 is involved in
CC control of translational fidelity.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000255|HAMAP-Rule:MF_01307}.
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DR EMBL; AL123456; CCP43465.1; -; Genomic_DNA.
DR PIR; D70644; D70644.
DR RefSeq; NP_215235.1; NC_000962.3.
DR RefSeq; WP_003403680.1; NZ_NVQJ01000007.1.
DR PDB; 7KGB; EM; 2.70 A; e=1-220.
DR PDB; 7MSC; EM; 2.97 A; e=1-220.
DR PDB; 7MSH; EM; 3.23 A; e=1-220.
DR PDB; 7MSM; EM; 2.79 A; e=1-220.
DR PDB; 7MSZ; EM; 3.10 A; e=1-220.
DR PDB; 7MT2; EM; 2.76 A; e=1-220.
DR PDB; 7MT3; EM; 2.80 A; e=1-220.
DR PDB; 7MT7; EM; 2.71 A; e=1-220.
DR PDBsum; 7KGB; -.
DR PDBsum; 7MSC; -.
DR PDBsum; 7MSH; -.
DR PDBsum; 7MSM; -.
DR PDBsum; 7MSZ; -.
DR PDBsum; 7MT2; -.
DR PDBsum; 7MT3; -.
DR PDBsum; 7MT7; -.
DR AlphaFoldDB; P9WH33; -.
DR SMR; P9WH33; -.
DR STRING; 83332.Rv0721; -.
DR iPTMnet; P9WH33; -.
DR PaxDb; P9WH33; -.
DR DNASU; 888465; -.
DR GeneID; 45424686; -.
DR GeneID; 888465; -.
DR KEGG; mtu:Rv0721; -.
DR TubercuList; Rv0721; -.
DR eggNOG; COG0098; Bacteria.
DR OMA; KRGCGSW; -.
DR PhylomeDB; P9WH33; -.
DR PRO; PR:P9WH33; -.
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:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005712; Ribosomal_S5_bac-type.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..220
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131556"
FT DOMAIN 42..105
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21969609"
SQ SEQUENCE 220 AA; 22888 MW; F40C104B499F7498 CRC64;
MAEQPAGQAG TTDNRDARGD REGRRRDSGR GSRERDGEKS NYLERVVAIN RVSKVVKGGR
RFSFTALVIV GDGNGMVGVG YGKAKEVPAA IAKGVEEARK SFFRVPLIGG TITHPVQGEA
AAGVVLLRPA SPGTGVIAGG AARAVLECAG VHDILAKSLG SDNAINVVHA TVAALKLLQR
PEEVAARRGL PIEDVAPAGM LKARRKSEAL AASVLPDRTI
