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Database: UniProt
Entry: A0A291GEB0_9RHOB
LinkDB: A0A291GEB0_9RHOB
Original site: A0A291GEB0_9RHOB 
ID   A0A291GEB0_9RHOB        Unreviewed;       433 AA.
AC   A0A291GEB0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=HslU--HslV peptidase ATPase subunit {ECO:0000313|EMBL:ATG48392.1};
GN   ORFNames=CEW89_12970 {ECO:0000313|EMBL:ATG48392.1};
OS   Celeribacter ethanolicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1758178 {ECO:0000313|EMBL:ATG48392.1, ECO:0000313|Proteomes:UP000217935};
RN   [1] {ECO:0000313|EMBL:ATG48392.1, ECO:0000313|Proteomes:UP000217935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSPH2 {ECO:0000313|EMBL:ATG48392.1,
RC   ECO:0000313|Proteomes:UP000217935};
RA   Woo J.-H., Kim H.-S.;
RT   "Celeribacter sp. TSPH2 complete genome sequence.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000256|ARBA:ARBA00009771}.
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DR   EMBL; CP022196; ATG48392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291GEB0; -.
DR   STRING; 1758178.GCA_001550095_04111; -.
DR   KEGG; ceh:CEW89_12970; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000217935; Chromosome.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   CDD; cd19498; RecA-like_HslU; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004491; HslU.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00390; hslU; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217935}.
FT   DOMAIN          49..322
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          325..419
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   433 AA;  48127 MW;  6FE1CA4C48651BE3 CRC64;
     MTDLTPREIV SELDRYIIGQ NDAKRAVAVA LRNRWRRKQL SDDLREEVYP KNILMIGPTG
     VGKTEISRRL AKLAKAPFVK VEATKFTEVG YVGRDVEQIV RDLVDAAISQ TRDQMREDVK
     AKAQGAAEDR VIEAIAGKDA REQTRDMFRK KLRSGELDDT VIELELQDTG MPMGMFEVPG
     QPQMGGMMNL GDLFKGLGGR TVKKRLTVAE SYDILIGEEA DKLLDDETVT RVALEAVQEN
     GIVFIDEIDK VCARSDARGG DVSREGVQRD LLPLIEGTTV STKHGPVKTD HILFIASGAF
     HIAKPSDLLP ELQGRLPIRV ELRALEEGDF VRILTETDNA LTLQYKALME TEEVDVTFTE
     DGIAAIAKLA ADVNTTVENI GARRLYTIME RVFEELSFVA PDKPGEKITV DAAYVHAHVD
     EMAKIADVSR YML
//
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