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Database: UniProt
Entry: A0A239TSB2_9FIRM
LinkDB: A0A239TSB2_9FIRM
Original site: A0A239TSB2_9FIRM 
ID   A0A239TSB2_9FIRM        Unreviewed;       441 AA.
AC   A0A239TSB2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:SNV00038.1};
GN   Name=clpX_2 {ECO:0000313|EMBL:SNV00038.1};
GN   ORFNames=SAMEA4364220_01240 {ECO:0000313|EMBL:SNV00038.1};
OS   Megamonas hypermegale.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Megamonas.
OX   NCBI_TaxID=158847 {ECO:0000313|EMBL:SNV00038.1, ECO:0000313|Proteomes:UP000215383};
RN   [1] {ECO:0000313|EMBL:SNV00038.1, ECO:0000313|Proteomes:UP000215383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10570 {ECO:0000313|EMBL:SNV00038.1,
RC   ECO:0000313|Proteomes:UP000215383};
RG   Pathogen Informatics;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT906446; SNV00038.1; -; Genomic_DNA.
DR   RefSeq; WP_027890589.1; NZ_NFIW01000009.1.
DR   AlphaFoldDB; A0A239TSB2; -.
DR   GeneID; 78507244; -.
DR   eggNOG; COG1219; Bacteria.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000215383; Chromosome 1.
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:SNV00038.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:SNV00038.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:SNV00038.1};
KW   Protease {ECO:0000313|EMBL:SNV00038.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215383}.
FT   DOMAIN          124..284
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          332..426
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   441 AA;  49752 MW;  465B848F63CED952 CRC64;
     MKKNSQEVKH NCSFCNRTIT IHSQYDMPIY DPQTGFAICK NCIKDIYNFI AEHDKREEKA
     VNRKFAESLD DILAKNKPHV IKEYLDQYII NQDYAKKILS VAVYNHYKRM KYGYTHDPKD
     MNIEKSNVIM LGPSGCGKTA MLQHLAKLLD IPMAVTDASS LTEAGFVGSD VEVAVRNLYY
     AADKNIERTE HGIIYLDEFD KIARKSGANN SITADPGHEG VQQGLLKMIE GGVVEFTAQG
     QRKHPEAPTI KVNTTNILFI VGGAFVGIED IIAKRLKTDA TSIGFGAEVQ NKNDKPKYNS
     LIHKVRPEDL IQFGIIPEII GRLPVICTLE ELSEDDLLKI LTEPKNAPVK QYQELLSMDN
     VKLEFEKDAL YAVAHKAIER KTGARSLRGI LEDVMLDIMY EIPQSNEPRR VIITKDCIEN
     HTKPEILPLE TSKTNKTTEN N
//
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