ID A0A147K5D4_9BACI Unreviewed; 816 AA.
AC A0A147K5D4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:KUP04816.1};
GN ORFNames=Q75_14420 {ECO:0000313|EMBL:KUP04816.1};
OS Bacillus coahuilensis p1.1.43.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP04816.1, ECO:0000313|Proteomes:UP000074108};
RN [1] {ECO:0000313|EMBL:KUP04816.1, ECO:0000313|Proteomes:UP000074108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA Olmedo-Alvarez G.;
RT "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT Phosphorus Acquisition Strategies and Their Regulation.";
RL Front. Microbiol. 7:58-58(2016).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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:KUP04816.1}.
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DR EMBL; LDYG01000047; KUP04816.1; -; Genomic_DNA.
DR RefSeq; WP_010170056.1; NZ_LDYG01000047.1.
DR AlphaFoldDB; A0A147K5D4; -.
DR STRING; 1150625.Q75_14420; -.
DR PATRIC; fig|1150625.3.peg.3016; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000074108; 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: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; 1.10.1780.10; Clp, N-terminal domain; 1.
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; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
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:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
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:KUP04816.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KUP04816.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000074108};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 417..452
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 413..459
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 816 AA; 90592 MW; D6E06D9D3F5629C4 CRC64;
MMFGRFTERA QKVLALAQEE AIRLSHSNIG TEHILLGLVR EGEGIAAKAL YALGLSSEKI
QKEVETLIGK GKETTQNIHY TPRAKKVIEL SMDEARKLGH SYVGTEHILL GLIREGEGVA
ARVLNNLGVS LNKARQQVLQ LLGSSESSSH QGGGNAGANT PTLDSLARDL TAIAREGSLD
PVIGRSKEIQ RVIEVLSRRT KNNPVLIGEP GVGKTAIAEG LAQQIIQNEV PEILRDKRVM
TLDMGTVVAG TKYRGEFEDR LKKVMDEIRQ AGNIILFIDE LHTLIGAGGA EGAIDASNIL
KPSLARGELQ CIGATTLDEY RKYIEKDAAL ERRFQPIQVD EPTVDESIQI LQGLRDRYEA
HHRVSITDAA IQAAVKLSDR YISDRFLPDK AIDLIDEAGS KVRLRSYTTP PNLKELEQRL
ETVRKEKDAA VQSQEFEKAA SLRDTEQKLR EELDSTKNTW KEKQGQENTE VTVDDIAHVV
SVWTGVPVSK IAQTETDKLL NLESILHSRV IGQEEAVKAV SKAVRRARAG LKDPKRPIGS
FIFLGPTGVG KTELARALAE AMFGDEDAMI RIDMSEYMEK HSTSRLVGSP PGYVGYDEGG
QLTEKVRRKP YSVILLDEIE KAHPDVFNIL LQVLEDGRLT DSKGRTVDFR NTVLIMTSNV
GASTLQRNKN VGFNVSDSGE DYKDMKGKVM EELKRAFRPE FLNRIDETIV FHSLEKAHLQ
EIVTLMSDQL TKRLIEQDIH LSLTDKAKDK IADEGFDPEY GARPLRRAIQ KHIEDRLSEE
LLKGTIITGQ NISIDVEEGE FKVNIQEPTE STTSNS
//