ID A0A1H7S9F1_9FIRM Unreviewed; 737 AA.
AC A0A1H7S9F1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SEL69175.1};
GN ORFNames=SAMN04487770_11533 {ECO:0000313|EMBL:SEL69175.1};
OS Butyrivibrio sp. ob235.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1761780 {ECO:0000313|EMBL:SEL69175.1, ECO:0000313|Proteomes:UP000199418};
RN [1] {ECO:0000313|EMBL:SEL69175.1, ECO:0000313|Proteomes:UP000199418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB235 {ECO:0000313|EMBL:SEL69175.1,
RC ECO:0000313|Proteomes:UP000199418};
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; FOBE01000015; SEL69175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7S9F1; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199418; 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 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 PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 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; 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.
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 Hydrolase {ECO:0000313|EMBL:SEL69175.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEL69175.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199418};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..141
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 737 AA; 82186 MW; BD84FFDEC174AF28 CRC64;
MNLSAEAMLA LQNAVEYASS NQYEYVTPEL VLLMMLDDEA FREAYEECGG DIQALSKNLM
NYAAKYIEKV KGKEPVLSLS TQHMINFAGQ SAYSSGCSEV HIRHLIHAIW NLDNSYAVYY
MEQDGLTEAE LLEELSYIED ENVDYGGSAS TGGPEREEDT GNLKIFAPCL NDTLEDVNPL
IGRKEELERT IQILCRKDKN NPLHIGEPGV GKTAITYGLV ELLRKNEVPD AIKGARVFAL
DLGGMLAGTQ YRGDFEKRFK KVLSEIGKEE KPIIYIDEIH NLSGAGAVGE GSFDASNMLK
PYLADGHIRF IGATTFEEYK KYFEKNKSLV RRFQNVEIKE PSEEESIRIL EGLKDKYENY
HGVIYEDEVL PYAVKMSAKY INERYLPDKA IDIIDEAGSF RKLHPLKAKK QIVDKEVINE
ILTKICRVPI ETVETDDVTG LATLENRLKG KIFGQDEAVS QVVNAVKFSK AGLSEENKPL
ASLLFVGPTG VGKTEIAKRL ADELGVKLIR FDMSEYGEKH AVAKLIGSPA GYVGYEEGGI
LTEAIRKSPS AVLLLDEIEK AHPDIYNVLL QVMDYATLTD NQGRKADFRN VVVIMTSNAG
ANKLGKSGIG FVSEGHDNSV LMEEVKRVFQ PEFRNRLSKV VVFNSMDEDM ASLVVDKKLS
ELKDQLSVKK IVFSADKKAK DLVIKRGISQ EFGAREVDRV IRNDIKPLFV DEILFGKLKN
GGKLTLTVKS GEFSVRT
//