(data stored in SCRATCH zone)

SWISSPROT: C8W402_DESAS

ID   C8W402_DESAS            Unreviewed;       166 AA.
AC   C8W402;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000256|HAMAP-Rule:MF_01307, ECO:0000256|SAAS:SAAS00085406};
GN   Name=rpsE {ECO:0000256|HAMAP-Rule:MF_01307};
GN   OrderedLocusNames=Dtox_0303 {ECO:0000313|EMBL:ACV61256.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61256.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61256.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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, ECO:0000256|SAAS:SAAS00085417}.
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000256|HAMAP-Rule:MF_01307,
CC       ECO:0000256|SAAS:SAAS00085429}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4
CC       and S8. {ECO:0000256|HAMAP-Rule:MF_01307,
CC       ECO:0000256|SAAS:SAAS00382311}.
CC   -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC       subunit; the C-terminal domain interacts with the body and
CC       contacts protein S4. The interaction surface between S4 and S5 is
CC       involved in control of translational fidelity. {ECO:0000256|HAMAP-
CC       Rule:MF_01307}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01307, ECO:0000256|RuleBase:RU003823,
CC       ECO:0000256|SAAS:SAAS00812081}.
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DR   EMBL; CP001720; ACV61256.1; -; Genomic_DNA.
DR   RefSeq; WP_015755977.1; NC_013216.1.
DR   STRING; 485916.Dtox_0303; -.
DR   EnsemblBacteria; ACV61256; ACV61256; Dtox_0303.
DR   KEGG; dae:Dtox_0303; -.
DR   eggNOG; ENOG4108RA9; Bacteria.
DR   eggNOG; COG0098; LUCA.
DR   HOGENOM; HOG000072595; -.
DR   KO; K02988; -.
DR   OMA; KRGCGSW; -.
DR   OrthoDB; 1505038at2; -.
DR   BioCyc; DACE485916:G1GFV-318-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
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; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005712; Ribosomal_S5_bac-type.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W402.
DR   SWISS-2DPAGE; C8W402.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01307,
KW   ECO:0000256|PROSITE-ProRule:PRU00268, ECO:0000256|RuleBase:RU003823,
KW   ECO:0000256|SAAS:SAAS00085448};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01307,
KW   ECO:0000256|PROSITE-ProRule:PRU00268, ECO:0000256|RuleBase:RU003823,
KW   ECO:0000256|SAAS:SAAS00085494};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01307,
KW   ECO:0000256|SAAS:SAAS00459555};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01307,
KW   ECO:0000256|SAAS:SAAS00459490}.
FT   DOMAIN       11     74       S5 DRBM. {ECO:0000259|PROSITE:PS50881}.
SQ   SEQUENCE   166 AA;  17290 MW;  1B68B454A8BEFD20 CRC64;
     MAAIDPNKLE LSEKIVYINR VAKVVKGGRR FSFSALVVVG DGNGHVGAGL GKAGEVPEAI
     RKGIEDAKKH LIRIPLSGTT IPHEVIGRFG AGRVLLKPAS AGTGVIAGGP VRAILELGGV
     RDILTKSLGS NNANNMVHAT MAAIESLKTP EEVARSRGKT LEELLS
//

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