ID M7N7I8_9FLAO Unreviewed; 174 AA.
AC M7N7I8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=D778_00696 {ECO:0000313|EMBL:EMQ94413.1}, DHV22_06785
GN {ECO:0000313|EMBL:HCY81312.1};
OS Xanthomarina gelatinilytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Xanthomarina.
OX NCBI_TaxID=1137281 {ECO:0000313|EMBL:EMQ94413.1, ECO:0000313|Proteomes:UP000012024};
RN [1] {ECO:0000313|EMBL:EMQ94413.1, ECO:0000313|Proteomes:UP000012024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK20 {ECO:0000313|EMBL:EMQ94413.1,
RC ECO:0000313|Proteomes:UP000012024};
RA Kumar R., Khatri I., Vaidya B., Subramanian S., Pinnaka A.;
RT "Genome assembly of Formosa sp. AK20.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HCY81312.1, ECO:0000313|Proteomes:UP000263268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBA10227 {ECO:0000313|EMBL:HCY81312.1};
RX PubMed=30148503; DOI=.1038/nbt.4229;
RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A.,
RA Chaumeil P.A., Hugenholtz P.;
RT "A standardized bacterial taxonomy based on genome phylogeny substantially
RT revises the tree of life.";
RL Nat. Biotechnol. 36:996-1004(2018).
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:EMQ94413.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ANLA01000016; EMQ94413.1; -; Genomic_DNA.
DR EMBL; DPRK01000112; HCY81312.1; -; Genomic_DNA.
DR RefSeq; WP_007650455.1; NZ_ANLA01000016.1.
DR STRING; 1137281.D778_00696; -.
DR PATRIC; fig|1137281.3.peg.2130; -.
DR eggNOG; COG0098; Bacteria.
DR OrthoDB; 9809045at2; -.
DR Proteomes; UP000012024; Unassembled WGS sequence.
DR Proteomes; UP000263268; 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:UP000012024};
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 18..81
FT /note="S5 DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50881"
SQ SEQUENCE 174 AA; 18230 MW; 8BF2EE2621C16225 CRC64;
MYQKYKSAEL VKPSGLDLKD RLVGVQRVTK VTKGGRAFGF SAIVVVGDEA GVVGHGLGKS
KDVASAIAKA VEDAKKNLVR IPLVKRSLPH EQKGKYGGAR VNIIPAAPGT GVIAGGAVRT
VLEAVGVHDV LSKSQGSSNP HNVVKATFDA LLQLRNANTI ARDRGISLEK VFKG
//
