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Database: UniProt
Entry: I0IMV4_LEPFC
LinkDB: I0IMV4_LEPFC
Original site: I0IMV4_LEPFC 
ID   I0IMV4_LEPFC            Unreviewed;       160 AA.
AC   I0IMV4;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Small ribosomal subunit protein uS5 {ECO:0000256|ARBA:ARBA00035255, ECO:0000256|HAMAP-Rule:MF_01307};
GN   Name=rpsE {ECO:0000256|HAMAP-Rule:MF_01307};
GN   OrderedLocusNames=LFE_0899 {ECO:0000313|EMBL:BAM06603.1};
OS   Leptospirillum ferrooxidans (strain C2-3).
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM06603.1, ECO:0000313|Proteomes:UP000007382};
RN   [1] {ECO:0000313|EMBL:BAM06603.1, ECO:0000313|Proteomes:UP000007382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2-3 {ECO:0000313|EMBL:BAM06603.1,
RC   ECO:0000313|Proteomes:UP000007382};
RX   PubMed=22815442; DOI=10.1128/JB.00696-12;
RA   Fujimura R., Sato Y., Nishizawa T., Oshima K., Kim S.-W., Hattori M.,
RA   Kamijo T., Ohta H.;
RT   "Complete Genome Sequence of Leptospirillum ferrooxidans Strain C2-3,
RT   Isolated from a Fresh Volcanic Ash Deposit on the Island of Miyake,
RT   Japan.";
RL   J. Bacteriol. 194:4122-4123(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382};
RA   Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M.,
RA   Kamijo T., Ohta H.;
RT   "The complete genome sequence of the pioneer microbe on fresh volcanic
RT   deposit, Leptospirillum ferrooxidans strain C2-3.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01307}.
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000256|HAMAP-Rule:MF_01307}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and
CC       S8. {ECO:0000256|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. {ECO:0000256|HAMAP-Rule:MF_01307}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000256|ARBA:ARBA00008945, ECO:0000256|HAMAP-Rule:MF_01307,
CC       ECO:0000256|RuleBase:RU003823}.
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DR   EMBL; AP012342; BAM06603.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0IMV4; -.
DR   STRING; 1162668.LFE_0899; -.
DR   KEGG; lfc:LFE_0899; -.
DR   eggNOG; COG0098; Bacteria.
DR   HOGENOM; CLU_065898_2_2_0; -.
DR   Proteomes; UP000007382; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR000851; Ribosomal_uS5.
DR   InterPro; IPR005712; Ribosomal_uS5_bac-type.
DR   InterPro; IPR005324; Ribosomal_uS5_C.
DR   InterPro; IPR013810; Ribosomal_uS5_N.
DR   InterPro; IPR018192; Ribosomal_uS5_N_CS.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR01021; rpsE_bact; 1.
DR   PANTHER; PTHR48277; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR   PANTHER; PTHR48277:SF1; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007382};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01307};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01307};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01307};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01307}.
FT   DOMAIN          10..73
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50881"
SQ   SEQUENCE   160 AA;  16877 MW;  4E96FC86F66D38D1 CRC64;
     MIPQTEPGTM KDKVVFINRV SKVVKGGKRF SFSALVVVGD GNGKVGFGKG KAGEVPDAIK
     KAVENAKKSM ISVPLRQTTV PHEVLGHFGA EDVMIKPASE GTGMIAGGAV RAVMEVLGVS
     NILCKSLGSG NPYNVVRATI DGLSQLHSYH EVMSERKSIN
//
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