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Database: UniProt
Entry: C7MFD8_BRAFD
LinkDB: C7MFD8_BRAFD
Original site: C7MFD8_BRAFD 
ID   C7MFD8_BRAFD            Unreviewed;       227 AA.
AC   C7MFD8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=Bfae_23630 {ECO:0000313|EMBL:ACU86155.1};
OS   Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG
OS   19847 / NBRC 14762 / NCIMB 9860 / 6-10).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU86155.1, ECO:0000313|Proteomes:UP000001919};
RN   [1] {ECO:0000313|EMBL:ACU86155.1, ECO:0000313|Proteomes:UP000001919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 /
RC   NCIMB 9860 / 6-10 {ECO:0000313|Proteomes:UP000001919};
RX   PubMed=21304631; DOI=10.4056/sigs.492;
RA   Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA   Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Brachybacterium faecium type strain
RT   (Schefferle 6-10).";
RL   Stand. Genomic Sci. 1:3-11(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}.
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; CP001643; ACU86155.1; -; Genomic_DNA.
DR   RefSeq; WP_015776360.1; NC_013172.1.
DR   RefSeq; YP_003155745.1; NC_013172.1.
DR   AlphaFoldDB; C7MFD8; -.
DR   STRING; 446465.Bfae_23630; -.
DR   KEGG; bfa:Bfae_23630; -.
DR   PATRIC; fig|446465.5.peg.2338; -.
DR   eggNOG; COG0098; Bacteria.
DR   HOGENOM; CLU_065898_2_1_11; -.
DR   OrthoDB; 9809045at2; -.
DR   Proteomes; UP000001919; 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:UP000001919};
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          51..114
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50881"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   227 AA;  23373 MW;  892C8D715E64D3E3 CRC64;
     MAAQQRNNGP AASGRRDANS NNSNDRGRQG GDRGGRQGGR GRGQDAEKSA FLERVVSINR
     VSKVVKGGRR FSFTALVVVG DGDGTVGVGY GKAKEVPAAI SKGVEEAKKN FFRVPRIQGT
     VVHPVQGEDA AGVVLLRPAA PGTGVIAGGP VRAVLECAGV HDVLSKSLGS TNQINIVRAT
     VDALKQLEEP EAVAARRGLA VEDVAPAALL RAQAEGRAAA RAEKVSA
//
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