(data stored in SCRATCH zone)

SWISSPROT: D3VH22_XENNA

ID   D3VH22_XENNA            Unreviewed;       443 AA.
AC   D3VH22;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
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   ECO:0000313|EMBL:CBJ88307.1};
GN   OrderedLocusNames=XNC1_0219 {ECO:0000313|EMBL:CBJ88307.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88307.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88307.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667742; CBJ88307.1; -; Genomic_DNA.
DR   RefSeq; WP_013183166.1; NC_014228.1.
DR   STRING; 406817.XNC1_0219; -.
DR   EnsemblBacteria; CBJ88307; CBJ88307; XNC1_0219.
DR   KEGG; xne:XNC1_0219; -.
DR   eggNOG; ENOG4105C4N; Bacteria.
DR   eggNOG; COG1220; LUCA.
DR   HOGENOM; HOG000010036; -.
DR   KO; K03667; -.
DR   OMA; KYGMIKT; -.
DR   Proteomes; UP000008075; 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; D3VH22.
DR   SWISS-2DPAGE; D3VH22.
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:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Hydrolase {ECO:0000313|EMBL:CBJ88307.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249,
KW   ECO:0000256|SAAS:SAAS00461902};
KW   Protease {ECO:0000313|EMBL:CBJ88307.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN       49    332       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      335    434       ClpB_D2-small. {ECO:0000259|SMART:
FT                                SM01086}.
FT   NP_BIND      60     65       ATP. {ECO:0000256|HAMAP-Rule:MF_00249}.
FT   COILED      192    212       {ECO:0000256|SAM:Coils}.
FT   BINDING      18     18       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00249}.
FT   BINDING     256    256       ATP. {ECO:0000256|HAMAP-Rule:MF_00249}.
FT   BINDING     321    321       ATP. {ECO:0000256|HAMAP-Rule:MF_00249}.
FT   BINDING     393    393       ATP. {ECO:0000256|HAMAP-Rule:MF_00249}.
SQ   SEQUENCE   443 AA;  50000 MW;  81A57740F956DBA9 CRC64;
     MSEMTPREIV SELDNHIIGQ DKAKRAVAIA LRNRWRRMQL DENLRYEVTP KNILMIGPTG
     VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDAAVKM VRLQSIEKNR
     YRAEELAEER ILDVLLPPAK NNWGQTETQS EPSSTRQAFR KKLREGQLDD KEIEIEVSAA
     PVGVEIMAPP GMEEMTNQLQ SMFQNMAGQR QKSRKLKIKD AFKLLVEEEA AKLVNPEELK
     QQAIDAVEQH GIVFIDEIDK ICKRGQTSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD
     HILFIASGAF QVSSPSDLIP ELQGRLPIRV ELQALTTEDF ERILTEPNAS LTEQYKALMA
     TEGMNIEFTA DGIRKIAEAA WQVNETTENI GARRLHTVLE RMMEDISFDA SERQGQFVEI
     NSDYVKENLD ELVANEDLSR FIL
//

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