ID N1V7G6_9MICC Unreviewed; 812 AA.
AC N1V7G6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=ATP-dependent Clp protease, ATP-binding subunit {ECO:0000313|EMBL:EMY34183.1};
GN ORFNames=D477_010851 {ECO:0000313|EMBL:EMY34183.1};
OS Arthrobacter crystallopoietes BAB-32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY34183.1, ECO:0000313|Proteomes:UP000010729};
RN [1] {ECO:0000313|EMBL:EMY34183.1, ECO:0000313|Proteomes:UP000010729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-32 {ECO:0000313|EMBL:EMY34183.1,
RC ECO:0000313|Proteomes:UP000010729};
RX PubMed=23833141;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT Revealing Genes for Bioremediation.";
RL Genome Announc. 1:e00452-13(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EMY34183.1}.
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DR EMBL; ANPE02000127; EMY34183.1; -; Genomic_DNA.
DR AlphaFoldDB; N1V7G6; -.
DR Proteomes; UP000010729; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR002078; Sigma_54_int.
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; PS50045; SIGMA54_INTERACT_4; 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:EMY34183.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EMY34183.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010729};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..123
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 401..436
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 494..759
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT COILED 397..443
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 812 AA; 89794 MW; 27F0B19692BBA55A CRC64;
MLNHNYIGTE HILLGLIHEG EGVAAKALEF LGVSLNGVRE QVQEIIGQGQ QAPSGHIPFT
PRAKKVLELS LREALQLGHN YIGTEHILLG LIREGEGVAT QVLVKLGADL NRVRQQVIQL
LSGYQGKEPV SAGGQQQEGA PAGSVVLDQF GRNLTQAARE SKLDPVIGRE HEMERVMQVL
SRRTKNNPVL IGEPGVGKTA VVEGLAQAIV RGDVPETIRD KQLYTLDLGS LVAGSRYRGD
FEERLKKVLK EIRTRGDIIL FIDEIHTLVG AGAAEGAIDA ASILKPMLAR GELQTIGATT
LDEYRKHIEK DAALERRFQP IQVNEPSVDH AVQILKGLRD RYEAHHRVSI TDGALDAAAH
LAHRYISDRF LPDKAIDLID EAGARLRIRR MTAPPELKEI DEKIAELKKQ KESAIDAQDF
EGAASLRDKE SKLQNERAAK ERAWKSGDLD EIAEVDEDLI AEVLANSTGI PVFKLTEEES
SRLMHMEAEL HKRVIGQDEA IKAISQAIRR TRAGLKDPNR PSGSFIFAGP TGVGKTELAK
ALAEFLFGEE DALITLDMSE YSEKHTVSRL FGAPPGYVGY EEGGQLTEKV RRRPFSVVLF
DEVEKAHADL FNSLLQILED GRLTDSQGRV VDFKNTVIIM TTNLGTRDIS KGVMTGFQSG
TDTKTGYERM RARVQDELKQ HFRPEFLNRV DDTVVFPQLT EEEIVQIVDL FVTRLQKRLA
EKNMKIDLTP AAKVLLANRG YDPTMGARPL RRTIQREVED QLSEKILFGE IQPGETIHVD
VDGEGDAAKL VFTTTGTPKA IEEAPETPAL SQ
//
