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Database: UniProt
Entry: H6LGT4_ACEWD
LinkDB: H6LGT4_ACEWD
Original site: H6LGT4_ACEWD 
ID   H6LGT4_ACEWD            Unreviewed;       168 AA.
AC   H6LGT4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
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   ECO:0000313|EMBL:AFA49598.1};
GN   OrderedLocusNames=Awo_c28470 {ECO:0000313|EMBL:AFA49598.1};
OS   Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS   / WB1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA49598.1, ECO:0000313|Proteomes:UP000007177};
RN   [1] {ECO:0000313|Proteomes:UP000007177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC   {ECO:0000313|Proteomes:UP000007177};
RA   Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA   Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT   "Complete genome sequence of Acetobacterium woodii.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFA49598.1, ECO:0000313|Proteomes:UP000007177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC   {ECO:0000313|Proteomes:UP000007177};
RX   PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA   Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA   Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA   Gottschalk G., Muller V.;
RT   "An ancient pathway combining carbon dioxide fixation with the generation
RT   and utilization of a sodium ion gradient for ATP synthesis.";
RL   PLoS ONE 7:E33439-E33439(2012).
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; CP002987; AFA49598.1; -; Genomic_DNA.
DR   RefSeq; WP_014357196.1; NC_016894.1.
DR   AlphaFoldDB; H6LGT4; -.
DR   STRING; 931626.Awo_c28470; -.
DR   KEGG; awo:Awo_c28470; -.
DR   eggNOG; COG0098; Bacteria.
DR   HOGENOM; CLU_065898_2_2_9; -.
DR   OrthoDB; 9809045at2; -.
DR   Proteomes; UP000007177; 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:UP000007177};
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          13..76
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50881"
SQ   SEQUENCE   168 AA;  17578 MW;  F560284A505B286D CRC64;
     MQNKKIDPST LDLKEKVVAI NRVTKVVKGG RNFRFSCLVI VGDENGHVGV GKGKAMEIPD
     AIRKGVDAAK KSLIKVPMVG TTIPHLVNGE AGAGHVLLKP AGKGTGVIAG GPVRAVLELA
     GIRDIRTKSL GSNNARNMVN ATMAGLAELT TLDEVAAKRG KKPEEILD
//
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