ID A0A4V2XIH0_9ACTN Unreviewed; 832 AA.
AC A0A4V2XIH0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:TDB98695.1};
GN ORFNames=E1267_38485 {ECO:0000313|EMBL:TDB98695.1};
OS Nonomuraea longispora.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1848320 {ECO:0000313|EMBL:TDB98695.1, ECO:0000313|Proteomes:UP000295157};
RN [1] {ECO:0000313|EMBL:TDB98695.1, ECO:0000313|Proteomes:UP000295157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC201 {ECO:0000313|EMBL:TDB98695.1,
RC ECO:0000313|Proteomes:UP000295157};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequences of novel Actinobacteria.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, 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:TDB98695.1}.
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DR EMBL; SMJZ01000239; TDB98695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V2XIH0; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000295157; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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.
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|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000313|EMBL:TDB98695.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TDB98695.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295157};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 44..187
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 181..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 832 AA; 91944 MW; 108BC05254268C8D CRC64;
MSDMPFRSFF GGDPFRGFEE LTGRVFGGME AWPPTRPSVQ RVDVGRLLSA SAREALRSAL
EKAGQRGAAD LDVLDLLGAL LDDDATGSML RSAGVDVGRL RDRIDALAGV GRPAEPPTTL
SPAAKRAILD AQRISRALQS SYIGPEHLLL ALPANPDSSA ARLLQEQGAS AGELQQAVVS
GGGARTGEQR MRNGDTPTLD EYGRDLTEEA RQGGIDPVVG REDEIEQCIE VLSRRTKNNP
CLIGEPGVGK TAIVEGIAQR IVNRTVPDIL KNRRVIGLDL TGMVAGTKYR GEFEERIKKV
IDEVRAHADE TIVFIDEVHN LVGAGSAEGG MDAANILKPA LARGELHVIA ATTIDEYRKN
IEKDAALERR FQPILVSEPT VEETIEILAG LRDTYEAHHQ VRITDEALDA AANLSARYVS
DRFLPDKAID LMDQASARVR LRSRTPGTGV RELEERLDSL RRDKDQAISA DDFDRAKELT
TEINKIRPEL ERARRGEDNV PQVGVEDIAE VVSRQTGIPV TQLTQHERER LMSLEEHLHK
RVIGQDEAVV AIAEAVRRAR AGLADPNRPI GSFLFLGPTG VGKTELARSL AAALFGGEDH
MVRIDMSEYQ ERHTVSRLIG APPGYVGYEE AGQLTEAVRR RPHGVILLDE IEKAHPDVMN
ILLQMLDDGR LTDGHGRTVD FTNAIVIMTS NIGAQMILGS EDTPELHDRL MDLLRHSLRP
ELLNRIDETI IFKRLERDQL RQIVDLLLER TRQRLRGQDV TMEVTDAAKD WLAERGYQPE
FGARPLRRTV QRELDNRLST MLLTGEIEEH GRVTVDVDGH GLQLRAHNPE QV
//