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Database: UniProt
Entry: M1M4Y9_9PROT
LinkDB: M1M4Y9_9PROT
Original site: M1M4Y9_9PROT 
ID   M1M4Y9_9PROT            Unreviewed;       444 AA.
AC   M1M4Y9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   13-SEP-2023, entry version 58.
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=CDSE_0127 {ECO:0000313|EMBL:AGF47235.1};
OS   Candidatus Kinetoplastibacterium desouzaii TCC079E.
OC   Bacteria; Pseudomonadota; Betaproteobacteria;
OC   Candidatus Kinetoplastibacterium.
OX   NCBI_TaxID=1208919 {ECO:0000313|EMBL:AGF47235.1, ECO:0000313|Proteomes:UP000011547};
RN   [1] {ECO:0000313|EMBL:AGF47235.1, ECO:0000313|Proteomes:UP000011547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCC079E {ECO:0000313|EMBL:AGF47235.1,
RC   ECO:0000313|Proteomes:UP000011547};
RX   PubMed=23345457;
RA   Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA   Teixeira M.M., Camargo E.P., Buck G.A.;
RT   "Genome evolution and phylogenomic analysis of candidatus
RT   kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT   and angomonas.";
RL   Genome Biol. Evol. 5:338-350(2013).
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; CP003803; AGF47235.1; -; Genomic_DNA.
DR   RefSeq; WP_015396646.1; NC_020294.1.
DR   AlphaFoldDB; M1M4Y9; -.
DR   STRING; 1208919.CDSE_0127; -.
DR   KEGG; kde:CDSE_0127; -.
DR   PATRIC; fig|1208919.3.peg.680; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_4; -.
DR   Proteomes; UP000011547; 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; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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:AGF47235.1};
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:AGF47235.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:AGF47235.1}.
FT   DOMAIN          52..333
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          336..430
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         63..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         257
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         322
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         394
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   444 AA;  50522 MW;  19BE67505E415AEB CRC64;
     MPSSTSMTPK EIVHQLDKHI IGQNRAKKAV AIALRNRWRR QQVPEELRQE IHPKNILMIG
     PTGVGKTEIA RRLAKLVDAP FIKIEATKFT EVGYVGRDVD TIIRDLIEQA VKEAREKEKK
     LIRSLAEEAA EERILDILIP PSSSNDNDQI TTDNTARQKF RKRLREGKID DLEIEISIPV
     ISTHLDVMTI PGMEEMADQI KTMFSGMTQD KKKNKKMQIK NAFKILVEEE ENRRINDDDI
     KSKAIKNVEQ NGIVFLDEID KIATRYGSDN AEVSRHGVQR DLLPLVEGTS VNTRYGVIKT
     DHVLFIASGA FHLSKPSDLI PELQGRFPIR VELDSLSIND FIHILRDTDS SLTKQYTSLL
     NTENINIQFS EDGIAKIANL AFYVNETNEN IGARRLYTVM EKLLENLSFE ASDMDGKDII
     INEKYVEEEL GQITSNQDLA KYIL
//
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