ID RS5_CHLTA Reviewed; 165 AA.
AC Q3KLI5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 01-MAY-2013, entry version 49.
DE RecName: Full=30S ribosomal protein S5;
GN Name=rpsE; OrderedLocusNames=CTA_0561;
OS Chlamydia trachomatis serovar A (strain HAR-13 / ATCC VR-571B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=315277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAR-13 / ATCC VR-571B;
RX PubMed=16177312; DOI=10.1128/IAI.73.10.6407-6418.2005;
RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT genitotropic strains.";
RL Infect. Immun. 73:6407-6418(2005).
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy (By similarity).
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 (By similarity).
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4
CC and S8 (By similarity).
CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC subunit; the C-terminal domain interacts with the body and
CC contacts protein S4. The interaction surface between S4 and S5 is
CC involved in control of translational fidelity.
CC -!- SIMILARITY: Belongs to the ribosomal protein S5P family.
CC -!- SIMILARITY: Contains 1 S5 DRBM domain.
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DR EMBL; CP000051; AAX50787.1; -; Genomic_DNA.
DR RefSeq; YP_328335.1; NC_007429.1.
DR ProteinModelPortal; Q3KLI5; -.
DR STRING; 315277.CTA_0561; -.
DR EnsemblBacteria; AAX50787; AAX50787; CTA_0561.
DR GeneID; 3688151; -.
DR KEGG; cta:CTA_0561; -.
DR PATRIC; 32023028; VBIChlTra31516_0573.
DR eggNOG; COG0098; -.
DR HOGENOM; HOG000072595; -.
DR KO; K02988; -.
DR OMA; HNVVKAT; -.
DR ProtClustDB; PRK00550; -.
DR BioCyc; CTRA315277:GI4C-587-MONOMER; -.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:HAMAP.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:HAMAP.
DR GO; GO:0006412; P:translation; IEA:HAMAP.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_01307_B; Ribosomal_S5_B; 1; -.
DR InterPro; IPR014720; dsRNA-bd-like_dom.
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; Ribosomal_S5_D2-typ_fold; 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 Complete proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1 165 30S ribosomal protein S5.
FT /FTId=PRO_0000230338.
FT DOMAIN 13 76 S5 DRBM.
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
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