ID A0A1A5XB81_9BACL Unreviewed; 220 AA.
AC A0A1A5XB81;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Small ribosomal subunit protein uS3 {ECO:0000256|ARBA:ARBA00035257, ECO:0000256|HAMAP-Rule:MF_01309};
GN Name=rpsC {ECO:0000256|HAMAP-Rule:MF_01309,
GN ECO:0000313|EMBL:UYZ13479.1};
GN ORFNames=A6764_00310 {ECO:0000313|EMBL:UYZ13479.1}, A6764_14360
GN {ECO:0000313|EMBL:OBR50440.1};
OS Brevibacillus sp. WF146.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=319501 {ECO:0000313|EMBL:OBR50440.1};
RN [1] {ECO:0000313|EMBL:OBR50440.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF146 {ECO:0000313|EMBL:OBR50440.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UYZ13479.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WF146 {ECO:0000313|EMBL:UYZ13479.1};
RA Tang B., Tang X.-F., Zhu F., Li Y.;
RT "Complete genome sequence of Brevibacillus thermoruber WF146.";
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in
CC the 70S ribosome, positioning it for translation.
CC {ECO:0000256|ARBA:ARBA00024998, ECO:0000256|HAMAP-Rule:MF_01309}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex with
CC proteins S10 and S14. {ECO:0000256|HAMAP-Rule:MF_01309}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000256|ARBA:ARBA00010761, ECO:0000256|HAMAP-Rule:MF_01309,
CC ECO:0000256|RuleBase:RU003624}.
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DR EMBL; LXGJ01000222; OBR50440.1; -; Genomic_DNA.
DR EMBL; CP109943; UYZ13479.1; -; Genomic_DNA.
DR RefSeq; WP_029101063.1; NZ_LXGJ01000222.1.
DR AlphaFoldDB; A0A1A5XB81; -.
DR Proteomes; UP000093585; Chromosome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
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 CDD; cd02412; KH-II_30S_S3; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.30.1140.32; Ribosomal protein S3, C-terminal domain; 1.
DR HAMAP; MF_01309_B; Ribosomal_S3_B; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR036419; Ribosomal_S3_C_sf.
DR InterPro; IPR005704; Ribosomal_uS3_bac-typ.
DR InterPro; IPR001351; Ribosomal_uS3_C.
DR InterPro; IPR018280; Ribosomal_uS3_CS.
DR NCBIfam; TIGR01009; rpsC_bact; 1.
DR PANTHER; PTHR11760:SF19; 30S RIBOSOMAL PROTEIN S3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR11760; 30S/40S RIBOSOMAL PROTEIN S3; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR SUPFAM; SSF54821; Ribosomal protein S3 C-terminal domain; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000093585};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01309};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01309};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01309};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01309}.
FT DOMAIN 38..106
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
SQ SEQUENCE 220 AA; 24253 MW; 355C2081E58C046E CRC64;
MGQKVSPVGL RIGIIRDWES KWYADKDFAT LLHEDLKIRK FIKGRLKDAA VSTIEIERAA
NRVNVTIHTA KPGMVIGKGG AEVEVLRKSL TELTGKRVHI NINEVKKPDL DATLVAENIA
RQLENRISFR RAQKQAISRT MRAGAKGIKT LVSGRLGGAD IARSEGYSEG TVPLHTLRAD
IDYGTAEAHT TYGRIGVKVW IYRGEVLPTK KNVATEEGGK
//
