ID G5H2J4_9FIRM Unreviewed; 430 AA.
AC G5H2J4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpX {ECO:0000313|EMBL:EHG24691.1};
GN ORFNames=HMPREF9432_01141 {ECO:0000313|EMBL:EHG24691.1};
OS Selenomonas noxia F0398.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=702437 {ECO:0000313|EMBL:EHG24691.1, ECO:0000313|Proteomes:UP000003175};
RN [1] {ECO:0000313|EMBL:EHG24691.1, ECO:0000313|Proteomes:UP000003175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0398 {ECO:0000313|EMBL:EHG24691.1,
RC ECO:0000313|Proteomes:UP000003175};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Selenomonas noxia F0398.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHG24691.1}.
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DR EMBL; ADGH01000010; EHG24691.1; -; Genomic_DNA.
DR RefSeq; WP_006696421.1; NZ_JH376859.1.
DR AlphaFoldDB; G5H2J4; -.
DR STRING; 702437.HMPREF9432_01141; -.
DR GeneID; 84787342; -.
DR PATRIC; fig|702437.3.peg.1151; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_9; -.
DR Proteomes; UP000003175; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00382; clpX; 1.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 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 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:EHG24691.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:EHG24691.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EHG24691.1};
KW Protease {ECO:0000313|EMBL:EHG24691.1}.
FT DOMAIN 122..349
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 330..424
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 430 AA; 47940 MW; F5AE6B5587624C0A CRC64;
MPKNPVKHQC SFCKRIIDVR DQYDMPIYDP NTGFAICKDC VREINRFLDE HDASVSSEER
TSFRMQLDDV LEKTRPHLIK EYLDSYIIKQ DRAKKILAVA VYNHYKRMKY GYEKEGEETE
IEKSNVIMLG PSGCGKTALL SHLSKLLDVP FAVTDASSLT EAGFVGADVE VAVRNLYYAA
DKDVERAEHG IIYLDEFDKI ARKSGANNSI TADPGHEGVQ QALLKMLEGS VVEFTARGQR
KHPEAPTIKV DTKNILFIVG GAFVGIEKVI SKRLKKGNVA IGFGAEVRGK DIEKEFDTLI
HQVTPEDLME YGIIPEIIGR LPVICTLETL DEDALLRILT EPINAPVRQY EKLLAMDGVE
LVFTEDALRA VAKKAIERKT GARSLKGIIE EVMLDVMFDI PRETAPRRVT VTKECITEGA
APIVEVAAAG
//
