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Database: UniProt
Entry: E4TSJ1_MARTH
LinkDB: E4TSJ1_MARTH
Original site: E4TSJ1_MARTH 
ID   E4TSJ1_MARTH            Unreviewed;       462 AA.
AC   E4TSJ1;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 67.
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   OrderedLocusNames=Ftrac_0809 {ECO:0000313|EMBL:ADR20811.1};
OS   Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408
OS   / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter tractuosus).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Marivirgaceae; Marivirga.
OX   NCBI_TaxID=643867 {ECO:0000313|EMBL:ADR20811.1, ECO:0000313|Proteomes:UP000008720};
RN   [1] {ECO:0000313|EMBL:ADR20811.1, ECO:0000313|Proteomes:UP000008720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 /
RC   H-43 {ECO:0000313|Proteomes:UP000008720};
RX   PubMed=21677852; DOI=10.4056/sigs.1623941;
RA   Pagani I., Chertkov O., Lapidus A., Lucas S., Del Rio T.G., Tice H.,
RA   Copeland A., Cheng J.F., Nolan M., Saunders E., Pitluck S., Held B.,
RA   Goodwin L., Liolios K., Ovchinikova G., Ivanova N., Mavromatis K., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Han C., Tapia R., Ngatchou-Djao O.D., Rohde M., Goker M., Spring S.,
RA   Sikorski J., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Marivirga tractuosa type strain (H-43).";
RL   Stand. Genomic Sci. 4:154-162(2011).
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; CP002349; ADR20811.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4TSJ1; -.
DR   STRING; 643867.Ftrac_0809; -.
DR   KEGG; mtt:Ftrac_0809; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_10; -.
DR   OMA; KYGMIKT; -.
DR   Proteomes; UP000008720; 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:InterPro.
DR   GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
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   Pfam; PF10431; ClpB_D2-small; 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};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00249};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008720};
KW   Stress response {ECO:0000313|EMBL:ADR20811.1}.
FT   DOMAIN          52..349
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          352..450
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         272
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         410
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   462 AA;  51630 MW;  3AC2AD60CF90742C CRC64;
     MNNNLFLTPK EIVAELDKYI IGQNDAKRNV AIALRNRWRR MNTPMDIQGE IVPNNILMIG
     ATGVGKTEIA RRLAKIADAP FTKVEASKFT EVGYVGRDVE SMVRDLVEQS VNLVKAAKKE
     EVKEKASQAV EDIILDALIP PMKSTNQRPV STTADNQVPD NDYELNQKTR ERFREKLRNG
     ELEDRKIDIN VKTPANNGMG MVGGGMMDEA SMINLQDMLS NMMPKKNKKR KVTIEEARKI
     LIDEEVSKLI DMDEVKEEAI KKAENTGMIF IDEIDKIAKG SGNSSGGDVS REGVQRDLLP
     IVEGSAVNTK YGIIHTDHIL FVAAGAFHVS KPSDLIPELQ GRFPIRVELD SLTKADFLRI
     LKEPKNALTK QYTALLKAEE VDLQFDDDAL EELAEIAYQV NSEVENIGAR RLQTVMSKLL
     NELLFDIPDK IGPNAKVVIT KQMVGEKLDG LVKDKDLSQY IL
//
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