RS5_CERSK
ID RS5_CERSK Reviewed; 187 AA.
AC B9KLA8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307};
GN OrderedLocusNames=RSKD131_0031;
OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/jb.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(2009).
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; CP001150; ACL99890.1; -; Genomic_DNA.
DR RefSeq; WP_002722522.1; NC_011963.1.
DR AlphaFoldDB; B9KLA8; -.
DR SMR; B9KLA8; -.
DR EnsemblBacteria; ACL99890; ACL99890; RSKD131_0031.
DR GeneID; 57469071; -.
DR GeneID; 67445517; -.
DR KEGG; rsk:RSKD131_0031; -.
DR HOGENOM; CLU_065898_2_2_5; -.
DR OMA; KRGCGSW; -.
DR Proteomes; UP000001597; Chromosome 1.
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..187
FT /note="30S ribosomal protein S5"
FT /id="PRO_1000165463"
FT DOMAIN 22..85
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 187 AA; 20623 MW; A1EC9489687B766E CRC64;
MAERENRRDR RDDRSREETP EFADRLVAIN RVSKTVKGGK RFGFAALVVV GDQRGRVGFG
KGKAKEVPEA IRKATEQAKR QMIRVALRDG RTLHHDQEGR HGAGKVVMRA AVPGTGIIAG
GPMRAVFEML GIQDVVAKSL GSQNPYNMIR ATMDGLKRES SPRQVAQRRG KKVADILKKP
EAEVAEA