RS5_ZYMMO
ID RS5_ZYMMO Reviewed; 233 AA.
AC Q5NQ48;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=ZMO0533;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}.
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:0000255|HAMAP-Rule:MF_01307}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and
CC S8. {ECO:0000255|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.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000255|HAMAP-Rule:MF_01307}.
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DR EMBL; AE008692; AAV89157.1; -; Genomic_DNA.
DR RefSeq; WP_011240440.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NQ48; -.
DR SMR; Q5NQ48; -.
DR STRING; 264203.ZMO0533; -.
DR EnsemblBacteria; AAV89157; AAV89157; ZMO0533.
DR GeneID; 58026371; -.
DR KEGG; zmo:ZMO0533; -.
DR eggNOG; COG0098; Bacteria.
DR HOGENOM; CLU_065898_2_1_5; -.
DR OMA; KRGCGSW; -.
DR OrthoDB; 1505038at2; -.
DR Proteomes; UP000001173; 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:InterPro.
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;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..233
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131642"
FT DOMAIN 59..122
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 233 AA; 24623 MW; B640AADFF2DAA16B CRC64;
MANESEIQKT ENAEVANAAN GTNPNNERRG RGGRGRGGRG RDGRGRRDDR RNEEAGEELI
EKLVHINRVS KTVKGGKRFG FAALVVVGDG KGRVGFGHGK AREVPEAISK ATAAAKKTMI
RVPLREGRTL HHDGRGRFGA GLVYLRSAPS GTGIIAGGPM RAIFESLGVA DVVTKSVGTS
NPYNMIRATF EALNDQKSPK AVAQRRGKRI ADLFGRGGAS AAKAEAEAAA VVE
