ID E8UBW3_DEIML Unreviewed; 178 AA.
AC E8UBW3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=Deima_2923 {ECO:0000313|EMBL:ADV68552.1};
OS Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 /
OS LB-34).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=709986 {ECO:0000313|EMBL:ADV68552.1, ECO:0000313|Proteomes:UP000008635};
RN [1] {ECO:0000313|EMBL:ADV68552.1, ECO:0000313|Proteomes:UP000008635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC {ECO:0000313|Proteomes:UP000008635};
RX PubMed=21677853; DOI=10.4056/sigs.1633949;
RA Pukall R., Zeytun A., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Deinococcus maricopensis type strain (LB-
RT 34).";
RL Stand. Genomic Sci. 4:163-172(2011).
RN [2] {ECO:0000313|Proteomes:UP000008635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC {ECO:0000313|Proteomes:UP000008635};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N.,
RA Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Pukall R., Gehrich-Schroeter G.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Deinococcus maricopensis DSM 21211.";
RL Submitted (JAN-2011) 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; CP002454; ADV68552.1; -; Genomic_DNA.
DR RefSeq; WP_013558056.1; NC_014958.1.
DR AlphaFoldDB; E8UBW3; -.
DR STRING; 709986.Deima_2923; -.
DR KEGG; dmr:Deima_2923; -.
DR eggNOG; COG0098; Bacteria.
DR HOGENOM; CLU_065898_2_2_0; -.
DR Proteomes; UP000008635; 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:UP000008635};
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 178 AA; 19058 MW; 76A94080316AAC4A CRC64;
MTFNRRPDRE RESSEFEEKM ISINRTAKTY QGGRRFRFAA LVIIGDRNGR VGMGIGKAKE
VPVAIEKAKA IARKNMITVP VENGTIPHDI VGEGTNSHVL LKPAAPGTGV IAGTVPRSIA
ELAGITNMLS KELGSRNQIN VAYAVFDGLK RLRTAKQVKA LRGTPAPAAP AQAEGSAQ
//
