GenomeNet

Database: UniProt
Entry: I4ZVY8_9GAMM
LinkDB: I4ZVY8_9GAMM
Original site: I4ZVY8_9GAMM 
ID   I4ZVY8_9GAMM            Unreviewed;       165 AA.
AC   I4ZVY8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
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:EIM40380.1};
GN   ORFNames=HADU_01597 {ECO:0000313|EMBL:EIM40380.1};
OS   Acinetobacter sp. HA.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1173062 {ECO:0000313|EMBL:EIM40380.1, ECO:0000313|Proteomes:UP000018434};
RN   [1] {ECO:0000313|EMBL:EIM40380.1, ECO:0000313|Proteomes:UP000018434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HA {ECO:0000313|EMBL:EIM40380.1,
RC   ECO:0000313|Proteomes:UP000018434};
RX   PubMed=22933775; DOI=10.1128/JB.01194-12;
RA   Malhotra J., Dua A., Saxena A., Sangwan N., Mukherjee U., Pandey N.,
RA   Rajagopal R., Khurana P., Khurana J.P., Lal R.;
RT   "Genome Sequence of Acinetobacter sp. Strain HA, Isolated from the Gut of
RT   the Polyphagous Insect Pest Helicoverpa armigera.";
RL   J. Bacteriol. 194:5156-5156(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|ARBA:ARBA00003093, 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIM40380.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJXD01000006; EIM40380.1; -; Genomic_DNA.
DR   RefSeq; WP_004657688.1; NZ_AJXD01000006.1.
DR   AlphaFoldDB; I4ZVY8; -.
DR   SMR; I4ZVY8; -.
DR   GeneID; 80104887; -.
DR   PATRIC; fig|1173062.3.peg.316; -.
DR   Proteomes; UP000018434; Unassembled WGS sequence.
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   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          10..73
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50881"
SQ   SEQUENCE   165 AA;  17140 MW;  5ADEF170997E9637 CRC64;
     MAKVEQNEGL VEKLVAVDRV AKVVKGGRIF SFTALTVVGD GNGRVGFGRG KAREVPAAIS
     KALEAARRNM ITVDLAGTTL QHPVNARHGA SRVYMQPASE GTGVIAGGAM RAVLEAAGVH
     NVLAKCYGST NAANVVNATF KGLRDMTSPE KVAAKRGLSV EQIQG
//
DBGET integrated database retrieval system