ID   HSLU_MANHA              Reviewed;         440 AA.
AC   P32180;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000255|HAMAP-Rule:MF_00249};
DE   AltName: Full=Unfoldase HslU {ECO:0000255|HAMAP-Rule:MF_00249};
GN   Name=hslU {ECO:0000255|HAMAP-Rule:MF_00249}; Synonyms=lapA;
OS   Mannheimia haemolytica (Pasteurella haemolytica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Mannheimia.
OX   NCBI_TaxID=75985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype A1 / PH101;
RX   PubMed=8359916; DOI=10.1128/iai.61.9.3942-3951.1993;
RA   Highlander S.K., Wickersham E.A., Garza O., Weinstock G.M.;
RT   "Expression of the Pasteurella haemolytica leukotoxin is inhibited by a
RT   locus that encodes an ATP-binding cassette homolog.";
RL   Infect. Immun. 61:3942-3951(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8359916.
RA   Highlander S.K., Wickersham E.A., Garza O., Weinstock G.M.;
RL   Infect. Immun. 61:5431-5431(1993).
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:0000255|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:0000255|HAMAP-
CC       Rule:MF_00249}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00249}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00249}.
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DR   EMBL; M59210; AAA25534.1; -; Genomic_DNA.
DR   PIR; S27609; S27609.
DR   RefSeq; WP_006248019.1; NZ_JAAAMS010000015.1.
DR   AlphaFoldDB; P32180; -.
DR   SMR; P32180; -.
DR   STRING; 75985.WC39_13350; -.
DR   MEROPS; X20.005; -.
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   Gene3D; 3.40.50.300; -; 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   PANTHER; PTHR48102:SF3; PTHR48102:SF3; 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; SSF52540; 1.
DR   TIGRFAMs; TIGR00390; hslU; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding.
FT   CHAIN           1..440
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_0000160527"
FT   REGION          141..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         59..64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         318
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         390
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   440 AA;  49693 MW;  9DF3BB1CFD63C15A CRC64;
     MSMTPREIVS ELDAHIIGQK DAKRAVAIAL RNRWRRMQLP EDLRQEVTPK NILMIGPTGV
     GKTEIARRLA KLANAPFIKV EATKFTEVGY VGKEVDSIIR DLADVSMKLV RQQAVEKNKM
     RAQDAAEDRI LDVLLPPAKD QWGNVQESDN NSTRQTFRKK LREGQLDDKE IEIDVAAQVS
     VEIMTPPGME EMTSQLQSLF EGMSPSKTKK RKMKIKDALK VMLDEEAAKL VNPEELKQQA
     IEAVEQHGIV FIDEIDKICK KGEHSGGDVS REGVQRDLLP IIEGSTVNTK HGMVKTDHIL
     FICSGAFQVA RPSDLLPELQ GRLPIRVELK SLTKEDFERI LTEPNASLTL QYRELMKTEG
     VEIEFTKDGI SRIAESAFRV NEKTENIGAR RLHTVLERLM DGISFDASER RGEKIIIDEN
     YVSEALNDVV ENEDLSRFIL