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Database: UniProt
Entry: R7JJP2_9BACT
LinkDB: R7JJP2_9BACT
Original site: R7JJP2_9BACT 
ID   R7JJP2_9BACT            Unreviewed;       172 AA.
AC   R7JJP2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
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   ORFNames=BN752_00468 {ECO:0000313|EMBL:CDE63906.1};
OS   Alistipes putredinis CAG:67.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1263036 {ECO:0000313|EMBL:CDE63906.1, ECO:0000313|Proteomes:UP000018026};
RN   [1] {ECO:0000313|EMBL:CDE63906.1, ECO:0000313|Proteomes:UP000018026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:67 {ECO:0000313|Proteomes:UP000018026};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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}.
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:CDE63906.1}.
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DR   EMBL; CBJI010000046; CDE63906.1; -; Genomic_DNA.
DR   RefSeq; WP_004329484.1; NZ_FR900700.1.
DR   AlphaFoldDB; R7JJP2; -.
DR   GeneID; 73803660; -.
DR   Proteomes; UP000018026; Unassembled WGS sequence.
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:UP000018026};
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          16..79
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50881"
SQ   SEQUENCE   172 AA;  18022 MW;  6E81630A7BB91DE6 CRC64;
     MANTNMKKVR TSDLELKDRL VSIQRVTKVT KGGRTFSFSA IVVVGNENGV VGYGLGKASE
     VTSAIAKGVE DAKKNLVKIP VINGTIPHKQ EMRFGGSLVM VRPAAPGTGI IAGGAMRAVL
     ESVGVKNVLA KSKGSSNPHN LVKATIAALC ELRDAHSVAQ LRGISMNQVF NG
//
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