ID A0A433HG94_9BACI Unreviewed; 218 AA.
AC A0A433HG94;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 16.
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 ORFNames=ELQ35_16050 {ECO:0000313|EMBL:RUQ27377.1};
OS Peribacillus cavernae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1674310 {ECO:0000313|EMBL:RUQ27377.1, ECO:0000313|Proteomes:UP000267430};
RN [1] {ECO:0000313|EMBL:RUQ27377.1, ECO:0000313|Proteomes:UP000267430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L5 {ECO:0000313|EMBL:RUQ27377.1,
RC ECO:0000313|Proteomes:UP000267430};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT Center where the Viking Spacecraft were Assembled.";
RL Submitted (DEC-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUQ27377.1}.
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DR EMBL; RYZZ01000027; RUQ27377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433HG94; -.
DR OrthoDB; 9806396at2; -.
DR Proteomes; UP000267430; Unassembled WGS sequence.
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:UP000267430};
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 218 AA; 24181 MW; 125CAAEC25F93930 CRC64;
MGQKVNPVGL RIGIIRDWES KWYAGKDYAT LLHEDLKVRE YIAKRLSDAS VSKVEIERAA
NRINISVHTA KPGMVIGKGG TEVEALRKAL NQLTAKRVHI NIIEIKRADL DAKLVAENIA
RQLENRVSFR RAQKQAIQRT MRAGAQGVRT QVSGRLGGAD IARAEHYSEG TVPLHTLRAD
IDYAAAEADT TYGKLGVKVW IYRGEVLPTK KKSEEGGK
//