ID W6TMX3_9SPIR Unreviewed; 208 AA.
AC W6TMX3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Small ribosomal subunit protein uS4 {ECO:0000256|ARBA:ARBA00035254, ECO:0000256|HAMAP-Rule:MF_01306};
GN Name=rpsD {ECO:0000256|HAMAP-Rule:MF_01306};
GN ORFNames=BDCR2A_00747 {ECO:0000313|EMBL:ETZ18774.1};
OS Borrelia duttonii CR2A.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borrelia.
OX NCBI_TaxID=1432657 {ECO:0000313|EMBL:ETZ18774.1, ECO:0000313|Proteomes:UP000019148};
RN [1] {ECO:0000313|EMBL:ETZ18774.1, ECO:0000313|Proteomes:UP000019148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR2A {ECO:0000313|EMBL:ETZ18774.1,
RC ECO:0000313|Proteomes:UP000019148};
RA Schwan T.G., Raffel S.J., Porcella S.F.;
RT "Comparative genomics of relapsing fever spirochetes.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01306}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC interaction surface between S4 and S5 is involved in control of
CC translational fidelity. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000256|ARBA:ARBA00007465, ECO:0000256|HAMAP-Rule:MF_01306,
CC ECO:0000256|RuleBase:RU003699}.
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:ETZ18774.1}.
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DR EMBL; AZIT01000001; ETZ18774.1; -; Genomic_DNA.
DR RefSeq; WP_012538359.1; NZ_AZIT01000001.1.
DR AlphaFoldDB; W6TMX3; -.
DR SMR; W6TMX3; -.
DR PATRIC; fig|1432657.3.peg.737; -.
DR Proteomes; UP000019148; Unassembled WGS sequence.
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 CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR InterPro; IPR022801; Ribosomal_uS4.
DR InterPro; IPR005709; Ribosomal_uS4_bac-type.
DR InterPro; IPR018079; Ribosomal_uS4_CS.
DR InterPro; IPR001912; Ribosomal_uS4_N.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR NCBIfam; TIGR01017; rpsD_bact; 1.
DR PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1.
DR PANTHER; PTHR11831:SF4; 37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019148};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01306};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01306};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01306};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01306}.
FT DOMAIN 3..94
FT /note="Small ribosomal subunit protein uS4 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01390"
FT DOMAIN 95..159
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
SQ SEQUENCE 208 AA; 23983 MW; FEB54C4BAE4A8090 CRC64;
MNRKSIAKGK LVRRFGVNIF EQPKYDKLLK KKPNPPGMHG RSRRTKVTEY GKQLIEKQKV
KFTYGVSERQ LTNVFKEARR QHGVTGDNLL ALLERRIDNI VYRAGFAISR AHARQIVSHG
IIILNGRRVT IPSITLRAND IIQVKEKDSL KKLVRSNIEK TSTLRKLPDW IEVNADALNV
KIIRTPSRDE IPTLANEQMI VEYYSKRA
//