(data stored in SCRATCH zone)

SWISSPROT: A0LEB6_SYNFM

ID   A0LEB6_SYNFM            Unreviewed;       466 AA.
AC   A0LEB6;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 96.
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=Sfum_0065 {ECO:0000313|EMBL:ABK15768.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15768.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15768.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex;
CC       this subunit has chaperone activity. The binding of ATP and its
CC       subsequent hydrolysis by HslU are essential for unfolding of
CC       protein substrates subsequently hydrolyzed by HslV. HslU
CC       recognizes the N-terminal part of its protein substrates and
CC       unfolds these before they are guided to HslV for hydrolysis.
CC       {ECO:0000256|HAMAP-Rule:MF_00249}.
CC   -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on
CC       each side by a ring-shaped HslU homohexamer. The assembly of the
CC       HslU/HslV complex is dependent on binding of ATP.
CC       {ECO:0000256|HAMAP-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|HAMAP-Rule:MF_00249, ECO:0000256|SAAS:SAAS00571467}.
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DR   EMBL; CP000478; ABK15768.1; -; Genomic_DNA.
DR   RefSeq; WP_011696941.1; NC_008554.1.
DR   STRING; 335543.Sfum_0065; -.
DR   EnsemblBacteria; ABK15768; ABK15768; Sfum_0065.
DR   KEGG; sfu:Sfum_0065; -.
DR   eggNOG; ENOG4105C4N; Bacteria.
DR   eggNOG; COG1220; LUCA.
DR   HOGENOM; HOG000010036; -.
DR   KO; K03667; -.
DR   OMA; KYGMIKT; -.
DR   OrthoDB; 718259at2; -.
DR   BioCyc; SFUM335543:G1G7I-67-MONOMER; -.
DR   Proteomes; UP000001784; 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:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro.
DR   GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
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; PTHR43815; PTHR43815; 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;
DR   PRODOM; A0LEB6.
DR   SWISS-2DPAGE; A0LEB6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00249,
KW   ECO:0000256|SAAS:SAAS00461882};
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00249,
KW   ECO:0000256|SAAS:SAAS00461921}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249,
KW   ECO:0000256|SAAS:SAAS00461902};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Stress response {ECO:0000313|EMBL:ABK15768.1}.
FT   DOMAIN       50    355       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      358    452       ClpB_D2-small. {ECO:0000259|SMART:
FT                                SM01086}.
FT   NP_BIND      61     66       ATP. {ECO:0000256|HAMAP-Rule:MF_00249}.
FT   COILED      163    183       {ECO:0000256|SAM:Coils}.
FT   BINDING      19     19       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00249}.
FT   BINDING     278    278       ATP. {ECO:0000256|HAMAP-Rule:MF_00249}.
FT   BINDING     344    344       ATP. {ECO:0000256|HAMAP-Rule:MF_00249}.
FT   BINDING     416    416       ATP. {ECO:0000256|HAMAP-Rule:MF_00249}.
SQ   SEQUENCE   466 AA;  53175 MW;  170D6DFD8F7CBB43 CRC64;
     MQKPLTPAEI VQELDKYIIG QRDAKRMVAI ALRNRWRRQQ VPEHLRDEIA PKNIIMIGPT
     GVGKTEIARR LARLAQSPFL KIEASKFTEV GYVGRDVESM IRDLSELAVS MVRTEEMEAV
     KIKAEELAEE KLLDILLPPK RQQESREQEL PVPVEPQEAR EPREAAREEA VQADSTREKL
     RKLLRKGALD DRYVELDVPD RNFPMVEIFA GTGMEDMDYN LRDMLGSMLP RRTKRRKVKI
     PEAREILVQE ESQRLIDMDK VIKSAIERVE HSGIIFLDEI DKIAGRESGG RGPDVSREGV
     QRDLLPIVEG STVTTKYGMV KTDHILFIAS GAFHISKPSD LIPELQGRFP IRVELASLTK
     EDFVRILKEP ENALIVQYKS LLATEEVELT FDDEAIEEIA GLAFQVNART ENIGARRLHT
     IMEKLLSDIS FNAPDLKGQK IPITRQYIQE TLSDIIKDED LSRYIL
//

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