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Database: UniProt
Entry: X4ZEC5_9BACL
LinkDB: X4ZEC5_9BACL
Original site: X4ZEC5_9BACL 
ID   X4ZEC5_9BACL            Unreviewed;       467 AA.
AC   X4ZEC5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000256|HAMAP-Rule:MF_00249};
DE   AltName: Full=Unfoldase HslU {ECO:0000256|HAMAP-Rule:MF_00249};
GN   Name=hslU {ECO:0000256|HAMAP-Rule:MF_00249};
GN   ORFNames=PSAB_14835 {ECO:0000313|EMBL:AHV97876.1};
OS   Paenibacillus sabinae T27.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV97876.1, ECO:0000313|Proteomes:UP000019772};
RN   [1] {ECO:0000313|EMBL:AHV97876.1, ECO:0000313|Proteomes:UP000019772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T27 {ECO:0000313|EMBL:AHV97876.1,
RC   ECO:0000313|Proteomes:UP000019772};
RX   PubMed=24651173;
RA   Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA   Chen X., Cheng Q., Chen S., Li J.;
RT   "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing Paenibacillus
RT   spp.: Organization, Evolution and Expression of the Nitrogen Fixation
RT   Genes.";
RL   PLoS Genet. 10:E1004231-E1004231(2014).
CC   -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; this
CC       subunit has chaperone activity. The binding of ATP and its subsequent
CC       hydrolysis by HslU are essential for unfolding of protein substrates
CC       subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of
CC       its protein substrates and unfolds these before they are guided to HslV
CC       for hydrolysis. {ECO:0000256|HAMAP-Rule:MF_00249}.
CC   -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on each
CC       side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV
CC       complex is dependent on binding of ATP. {ECO:0000256|HAMAP-
CC       Rule:MF_00249}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000256|ARBA:ARBA00009771, ECO:0000256|HAMAP-Rule:MF_00249}.
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DR   EMBL; CP004078; AHV97876.1; -; Genomic_DNA.
DR   RefSeq; WP_025335379.1; NZ_CP004078.1.
DR   AlphaFoldDB; X4ZEC5; -.
DR   STRING; 1268072.PSAB_14835; -.
DR   KEGG; psab:PSAB_14835; -.
DR   PATRIC; fig|1268072.3.peg.3068; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_9; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000019772; Chromosome.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00249; HslU; 1.
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|HAMAP-Rule:MF_00249, ECO:0000313|EMBL:AHV97876.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00249};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Hydrolase {ECO:0000313|EMBL:AHV97876.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:AHV97876.1}.
FT   DOMAIN          51..356
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          359..453
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          156..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         62..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         417
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   467 AA;  52358 MW;  663DE85E1083660E CRC64;
     MVNQSLTPRQ IVAELDKYIV GQKQAKKSMA VALRNRYRRG KLSEELRDEI VPKNILMIGP
     TGVGKTEIAR RLAKLVNAPF VKVEATKFTE VGYVGRDVES MVRDLVETAI RMVKLERTEK
     VKDRAEELAN ERIVRILAPS GSKNKAQRNP FEMLFGAGGN QEDAKPEDTD GDASLNERRR
     GIRFKLLAGQ MEDDVIEIDV EDTTPTMLDM FAGQGNDQMG MNMQEMFGSL LPKRTKKRKL
     PIREARKVLI QDEANKLIDM DDVIQESVAR AEQNGIIFID EIDKVASQGK GGGPDVSREG
     VQRDILPIVE GSTVMTKYGP VKTDYVLFVA AGAFHVAKPS DLIPELQGRF PIRVELSSLS
     LEDFVSILTE PKNALTKQYA HLLATEDIEV EFTKEAIYEI AKIAATVNQN MENIGARRLH
     TILEKLLEDL SFEAPELTLD KMVITPEYVR EKLASIAQDR DLSQYIL
//
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