(data stored in SCRATCH zone)

SWISSPROT: A0LEF0_SYNFM

ID   A0LEF0_SYNFM            Unreviewed;       417 AA.
AC   A0LEF0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS01076755};
GN   Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN   OrderedLocusNames=Sfum_0099 {ECO:0000313|EMBL:ABK15802.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15802.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15802.1, 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: ATP-dependent specificity component of the Clp protease.
CC       It directs the protease to specific substrates. Can perform
CC       chaperone functions in the absence of ClpP. {ECO:0000256|HAMAP-
CC       Rule:MF_00175, ECO:0000256|SAAS:SAAS01076750}.
CC   -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric
CC       ring that, in the presence of ATP, binds to fourteen ClpP subunits
CC       assembled into a disk-like structure with a central cavity,
CC       resembling the structure of eukaryotic proteasomes.
CC       {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00561096}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family.
CC       {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS01090919}.
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DR   EMBL; CP000478; ABK15802.1; -; Genomic_DNA.
DR   RefSeq; WP_011696975.1; NC_008554.1.
DR   STRING; 335543.Sfum_0099; -.
DR   EnsemblBacteria; ABK15802; ABK15802; Sfum_0099.
DR   KEGG; sfu:Sfum_0099; -.
DR   eggNOG; ENOG4105CHN; Bacteria.
DR   eggNOG; COG1219; LUCA.
DR   HOGENOM; HOG000010093; -.
DR   KO; K03544; -.
DR   OMA; DIMYDLP; -.
DR   OrthoDB; 718259at2; -.
DR   BioCyc; SFUM335543:G1G7I-103-MONOMER; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.50.30; -; 1.
DR   HAMAP; MF_00175; ClpX; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   InterPro; IPR038366; Znf_CppX_C4_sf.
DR   PANTHER; PTHR11262; PTHR11262; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF06689; zf-C4_ClpX; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00994; zf-C4_ClpX; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00382; clpX; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LEF0.
DR   SWISS-2DPAGE; A0LEF0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00089772, ECO:0000313|EMBL:ABK15802.1};
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00326717};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Hydrolase {ECO:0000313|EMBL:ABK15802.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00448062};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00089789};
KW   Protease {ECO:0000313|EMBL:ABK15802.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00448058};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00063417}.
FT   DOMAIN       11     50       zf-C4_ClpX. {ECO:0000259|SMART:SM00994}.
FT   DOMAIN      109    329       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      313    407       ClpB_D2-small. {ECO:0000259|SMART:
FT                                SM01086}.
FT   ZN_FING      14     39       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00175}.
FT   NP_BIND     118    125       ATP. {ECO:0000256|HAMAP-Rule:MF_00175}.
SQ   SEQUENCE   417 AA;  46438 MW;  318C8E4380930C0A CRC64;
     MARKRDDRGG ELRCSFCGKS QDEVKKLIAG PTVYICDECV ELCNDIIAEE YEREEAARAT
     QIPKPAEIKA ILDQYVIGQD RAKKILSVAV HNHYKRIELK IDKNDVELQK SNILMIGPTG
     SGKTLLAQTL ARILNVPFTI ADATTLTEAG YVGEDVENIL VSLIQAADYD IEKASRGIVY
     IDEIDKIAKK SDSPSITRDV SGEGVQQALL KILEGTVANV PPKGGRKHPQ QEFIKIDTTN
     ILFICGGAFN YLETIIQSRV GVKGMGFGAE IRSKEDKSVG EILIKVQPED LLKFGMIPEF
     VGRLPVIATL NELTEDELVS ILTEPKNALV KQYKKLFELE DVRLRFTEGV LRAIAKEAIR
     RKSGARGLRS IMENIMLDIM YDLPSHPEIQ ECIINEDVLV KQAKPLLLYR NQSQESA
//

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