ID A0A1G9IR43_9CLOT Unreviewed; 811 AA.
AC A0A1G9IR43;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SDL27334.1};
GN ORFNames=SAMN05660472_02921 {ECO:0000313|EMBL:SDL27334.1};
OS Natronincola ferrireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Natronincola.
OX NCBI_TaxID=393762 {ECO:0000313|EMBL:SDL27334.1, ECO:0000313|Proteomes:UP000198718};
RN [1] {ECO:0000313|EMBL:SDL27334.1, ECO:0000313|Proteomes:UP000198718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18346 {ECO:0000313|EMBL:SDL27334.1,
RC ECO:0000313|Proteomes:UP000198718};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FNFP01000012; SDL27334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9IR43; -.
DR STRING; 393762.SAMN05660472_02921; -.
DR Proteomes; UP000198718; 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: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; 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:SDL27334.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDL27334.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198718};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 4..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 419..454
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 145..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 415..461
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 811 AA; 90956 MW; D069627AF7EF9EC4 CRC64;
MSMHGRFTER AQQAIILSQQ YAQQLGHSYV GTEHLLLGLL QEGEGIAAKV LKNLKVETSQ
LQEKIISTVG KGLPQQLMGF TPRTKRVFEL SLEEARGLGH NYIGTEHLLL GLLREKEGVA
AKVLLEMGVQ LEKVKADVLK LLNNRGSQNN HRDHEKMGQG NTPTLDKYSR DLNKMAKEGK
IDPVIGRSQE IQRVIQILSR RTKNNPCLVG EPGVGKTAVA EGLAQQIIEG NVPEILKNKR
VVTLDLSSLL AGAKYRGEFE DRLKKVMEEI RQAGDIIIFI DEIHTMIGAG AAEGAIDASN
ILKPALARGE LQTIGATTID EYRKHIEKDA ALERRFQPIT IAEPSVEDTI KILEGLRDKY
EAHHTVKITD EAIKAAAELS HRYITDRFLP DKAIDLIDEA GSKIRLKTVT APPGLKDLEE
ELERLGKEKE EAISLQDFER AAEIRDKEKS IQQELQERQN TWQNKNLGDK AIVDGEEIAD
IVSQWTGVPV TKLQQEESER LLKMEKILHE RVIGQEEAVK SVSRAIRRAR VGLKDPKKPI
GSFIFLGPTG VGKTELSRAL AEAMFGEEDA MIRIDMSEYM EKHTVSRLIG SPPGYVGFDE
GGQLTEKVRR KPYSVILFDE IEKAHPDVFN VLLQILDDGR LTDAKGKTVD FKNTIIIMTS
NVGAHTIKKQ KTLGFAVSQE DMAKNEYEKM KENVMEELRK SFKPEFLNRI DDIIVFHSLD
KEYVSKIVDL MVEDLKNRLE KLDIKIDITD AAKAHIAEKG YDPQFGARPL KRAIQKLVED
RLSEELLKGT VVAGGHVEVD VENEELIVKQ K
//
