GenomeNet

Database: UniProt
Entry: I4VNL1_9GAMM
LinkDB: I4VNL1_9GAMM
Original site: I4VNL1_9GAMM 
ID   I4VNL1_9GAMM            Unreviewed;       108 AA.
AC   I4VNL1;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=ATP-dependent Clp protease adapter protein ClpS {ECO:0000256|HAMAP-Rule:MF_00302};
GN   Name=clpS {ECO:0000256|HAMAP-Rule:MF_00302};
GN   ORFNames=UU9_11180 {ECO:0000313|EMBL:EIL88802.1};
OS   Rhodanobacter fulvus Jip2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL88802.1, ECO:0000313|Proteomes:UP000004210};
RN   [1] {ECO:0000313|EMBL:EIL88802.1, ECO:0000313|Proteomes:UP000004210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX   PubMed=22843592; DOI=10.1128/JB.00871-12;
RA   Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA   Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA   Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT   "Genome sequences for six rhodanobacter strains, isolated from soils and
RT   the terrestrial subsurface, with variable denitrification capabilities.";
RL   J. Bacteriol. 194:4461-4462(2012).
CC   -!- FUNCTION: Involved in the modulation of the specificity of the ClpAP-
CC       mediated ATP-dependent protein degradation. {ECO:0000256|HAMAP-
CC       Rule:MF_00302}.
CC   -!- SUBUNIT: Binds to the N-terminal domain of the chaperone ClpA.
CC       {ECO:0000256|HAMAP-Rule:MF_00302}.
CC   -!- SIMILARITY: Belongs to the ClpS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00302}.
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:EIL88802.1}.
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; AJXU01000044; EIL88802.1; -; Genomic_DNA.
DR   RefSeq; WP_007081869.1; NZ_AJXU01000044.1.
DR   AlphaFoldDB; I4VNL1; -.
DR   STRING; 1163408.UU9_11180; -.
DR   PATRIC; fig|1163408.3.peg.2287; -.
DR   eggNOG; COG2127; Bacteria.
DR   OrthoDB; 9796121at2; -.
DR   Proteomes; UP000004210; Unassembled WGS sequence.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1390.10; -; 1.
DR   HAMAP; MF_00302; ClpS; 1.
DR   InterPro; IPR022935; ClpS.
DR   InterPro; IPR003769; ClpS_core.
DR   InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR   PANTHER; PTHR33473; ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR33473:SF20; ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS1, CHLOROPLASTIC; 1.
DR   Pfam; PF02617; ClpS; 1.
DR   SUPFAM; SSF54736; ClpS-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004210}.
FT   DOMAIN          26..104
FT                   /note="Adaptor protein ClpS core"
FT                   /evidence="ECO:0000259|Pfam:PF02617"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   108 AA;  12289 MW;  F27B139B6D1682E5 CRC64;
     MAHESEHEHD HGRGLAVESA KPEVARPPLF RVLLLNDDFT PMDFVVEVLR GFFNLDQEQA
     VQVMLHVHTR GRGVCGVFTR EVAETKVTQV NEYSRAHQHP LLCTMEKA
//
DBGET integrated database retrieval system