ID   A8FCH7_BACP2            Unreviewed;       700 AA.
AC   A8FCH7;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:ABV61944.1};
GN   OrderedLocusNames=BPUM_1261 {ECO:0000313|EMBL:ABV61944.1};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV61944.1, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ABV61944.1, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV61944.1,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP000813; ABV61944.1; -; Genomic_DNA.
DR   RefSeq; WP_012009743.1; NC_009848.4.
DR   AlphaFoldDB; A8FCH7; -.
DR   STRING; 315750.BPUM_1261; -.
DR   KEGG; bpu:BPUM_1261; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_3_9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000001355; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:ABV61944.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ABV61944.1}.
FT   DOMAIN          325..360
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          321..367
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   700 AA;  78025 MW;  69F8196359E3D3F5 CRC64;
     MRCQHCQVNE ATIRLNMQVN SSRSQMVLCE DCYTSLMEQS KMKMGPQLFG GSSFFSEQAG
     HTQNVEQPKH KGLLDELGRN LTDGANAGLI DPVIGRDEEV ARVIEILNRR NKNNPVLIGE
     PGVGKTAIAE GLALKIASGD VPNKLKNKQI YLLDVSSLVA NTGIRGQFEE RMKQLIKELQ
     SRKNIILFVD EIHLLVGAGS AEGSMDAGNI LKPALARGEL QLVGATTLKE YRQIEKDAAL
     ERRFQPVIVD EPTQAEAIEI LKGIQDKYES YHGITYSDEA IQACVQLSSR YIQDRHLPDK
     AIDLMDEAGS KANLSIDAAS EDELTNRLSE IAAEKQAALK EEQYEKAAKL RDEEEAIEAR
     LQNKTNHKEH VVTAEDIQAI VEQKTGIPVG KLQADEQTKM KEIDVRLKAR VIGQEHAVEK
     VAKAVKRSRA GLKSKHRPTG SFLFVGPTGV GKTELSKTLA EELFGSREAI IRLDMSEYME
     KHSVSKLIGS PPGYVGHDEA GQLTEKVRRK PYSIILLDEI EKAHPDVQHM FLQIMEDGRL
     TDSQGRTVSF KDTVIIMTSN AGSTDKTVKV GFQSDQEEAI EEQSLIDSLS AYFKPEFLNR
     FDSIIQFDSL DRDDLVKIVD LLLNELSAQL KEQNLTVHVT KEAKEKIAEL GYHPAFGARP
     LRRTIQEHVE DQMTEILLEE DKLLGFTVDV EDNEIVVKKG
//