RS5_CHLPB
ID RS5_CHLPB Reviewed; 172 AA.
AC B3EP44;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307};
GN OrderedLocusNames=Cphamn1_2279;
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001101; ACE05183.1; -; Genomic_DNA.
DR RefSeq; WP_012475646.1; NC_010831.1.
DR AlphaFoldDB; B3EP44; -.
DR SMR; B3EP44; -.
DR STRING; 331678.Cphamn1_2279; -.
DR KEGG; cpb:Cphamn1_2279; -.
DR eggNOG; COG0098; Bacteria.
DR HOGENOM; CLU_065898_2_2_10; -.
DR OMA; KRGCGSW; -.
DR OrthoDB; 1505038at2; -.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
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 Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..172
FT /note="30S ribosomal protein S5"
FT /id="PRO_1000140849"
FT DOMAIN 16..79
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
SQ SEQUENCE 172 AA; 18115 MW; CD5BEF97F0434F4F CRC64;
MAKRTANNIK PGELNLKEKL VHINRTAKVV KGGKRFGFNA IVVVGDKEGH VGFGLGKANE
VQDAIAKGVE DGKKNVIKVP IVKGTIPHQI IARYGSAKVM MKPATPGTGL IAGGAVRAVL
EMAGIHDILA KSLGSSNPHN VVKAAISGLE SISDAYDVAE RRSKSLKEVF ES