RS5_CHLTR
ID RS5_CHLTR Reviewed; 165 AA.
AC P0A4C8; P28543;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; Synonyms=rs5;
GN OrderedLocusNames=CT_512;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=L2/434/Bu;
RX PubMed=1735714; DOI=10.1128/jb.174.4.1205-1212.1992;
RA Kaul R., Gray G.J., Koehncke N.R., Gu L.J.;
RT "Cloning and sequence analysis of the Chlamydia trachomatis spc ribosomal
RT protein gene cluster.";
RL J. Bacteriol. 174:1205-1212(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; M80325; AAA23178.1; -; Genomic_DNA.
DR EMBL; AE001273; AAC68113.1; -; Genomic_DNA.
DR PIR; A45192; A45192.
DR RefSeq; NP_220027.1; NC_000117.1.
DR RefSeq; WP_009871876.1; NC_000117.1.
DR AlphaFoldDB; P0A4C8; -.
DR SMR; P0A4C8; -.
DR STRING; 813.O172_02825; -.
DR EnsemblBacteria; AAC68113; AAC68113; CT_512.
DR GeneID; 1246166; -.
DR GeneID; 884297; -.
DR KEGG; ctr:CT_512; -.
DR PATRIC; fig|272561.5.peg.556; -.
DR HOGENOM; CLU_065898_2_2_0; -.
DR InParanoid; P0A4C8; -.
DR OMA; KRGCGSW; -.
DR PRO; PR:P0A4C8; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
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 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..165
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131500"
FT DOMAIN 13..76
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
SQ SEQUENCE 165 AA; 17762 MW; 66F3E0AA8409481A CRC64;
MTLSRNSHKE DQLEEKVLVV NRCCKVVKGG RKFSFSALIL VGDRKGRLGF GFAKANELTD
AIRKGGDAAR KNLVSINSLE GGSIPHEVLV NHDGAELLLK PAKPGTGIVA GSRIRLILEM
AGVKDIVAKS LGSNNPMNQV KAAFKALLTL SCKDDIMKRR AVIND