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Database: UniProt
Entry: A0A095BRP7_9SPHN
LinkDB: A0A095BRP7_9SPHN
Original site: A0A095BRP7_9SPHN 
ID   A0A095BRP7_9SPHN        Unreviewed;       433 AA.
AC   A0A095BRP7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=ATP-dependent protease ATP-binding subunit HslU {ECO:0000313|EMBL:KGB53691.1};
GN   Name=hslU {ECO:0000313|EMBL:KGB53691.1};
GN   ORFNames=FG95_03101 {ECO:0000313|EMBL:KGB53691.1};
OS   Sphingopyxis sp. LC363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB53691.1, ECO:0000313|Proteomes:UP000029625};
RN   [1] {ECO:0000313|EMBL:KGB53691.1, ECO:0000313|Proteomes:UP000029625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC363 {ECO:0000313|EMBL:KGB53691.1,
RC   ECO:0000313|Proteomes:UP000029625};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000256|ARBA:ARBA00009771}.
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:KGB53691.1}.
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DR   EMBL; JNFC01000045; KGB53691.1; -; Genomic_DNA.
DR   RefSeq; WP_037557003.1; NZ_JNFC01000045.1.
DR   AlphaFoldDB; A0A095BRP7; -.
DR   STRING; 1120705.FG95_03101; -.
DR   PATRIC; fig|1120705.3.peg.3114; -.
DR   eggNOG; COG1220; Bacteria.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000029625; Unassembled WGS sequence.
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:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:KGB53691.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:KGB53691.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:KGB53691.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029625}.
FT   DOMAIN          50..322
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          325..421
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   433 AA;  47431 MW;  00EF70F3AAF12B67 CRC64;
     MNKDLTPKAI VAALDTHIIG QTAAKRAVAV ALRNRWRRQQ LSPDLRDEVS PKNILMIGPT
     GCGKTEISRR LAKLADAPFI KVEATKFTEV GYVGRDVEQI ARDLVEEAVR LEKDRRREAV
     RAAAEEAAME RLLDALTGKG ASEATRQSFR QRIREGHLDE SEVEIEVADT PSMNFELPGQ
     PGQMSMINLS DMLGKAMGGP PKKRRKLKVI EAATRLIEEE QDKRLDQDDV ARVALADAEA
     NGIVFLDEID KIAVSDVRGG SVSREGVQRD LLPLIEGTTV ATKYGPMKTD HILFIASGAF
     HVAKPSDLLP ELQGRLPIRV ELGALSEEDF VRILSETKAG LPEQYAALLG TEGVTLNFTD
     DAITRVARLA AEVNEKVENI GARRLQTIME RLVEEISFTA EDAGGTTLDI DAAYVDSQLA
     DVVGDTDLSK YVL
//
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