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Database: UniProt
Entry: A0A0C1U5F0_9CLOT
LinkDB: A0A0C1U5F0_9CLOT
Original site: A0A0C1U5F0_9CLOT 
ID   A0A0C1U5F0_9CLOT        Unreviewed;       809 AA.
AC   A0A0C1U5F0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=IstB-like ATP binding family protein {ECO:0000313|EMBL:KIE47954.1};
GN   ORFNames=U732_3486 {ECO:0000313|EMBL:KIE47954.1};
OS   Clostridium argentinense CDC 2741.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE47954.1, ECO:0000313|Proteomes:UP000031366};
RN   [1] {ECO:0000313|EMBL:KIE47954.1, ECO:0000313|Proteomes:UP000031366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE47954.1,
RC   ECO:0000313|Proteomes:UP000031366};
RX   PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA   Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA   Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA   Karavis M.A., Smith L.A.;
RT   "Genomic sequences of six botulinum neurotoxin-producing strains
RT   representing three clostridial species illustrate the mobility and
RT   diversity of botulinum neurotoxin genes.";
RL   Infect. Genet. Evol. 30:102-113(2014).
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:KIE47954.1}.
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DR   EMBL; AYSO01000013; KIE47954.1; -; Genomic_DNA.
DR   RefSeq; WP_039630622.1; NZ_AYSO01000013.1.
DR   AlphaFoldDB; A0A0C1U5F0; -.
DR   STRING; 29341.RSJ17_03490; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000031366; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; 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; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031366};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          418..453
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          414..460
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        145..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  90723 MW;  3B77B6BD07A9BBEF CRC64;
     MFNRFTERAR NILMYAHEES QNFKHGYVGT EHIILGILKE EESIAASALI NAGVDYNKVK
     ELVNKYIGVG DIEMPKNEIA LTPRTKRLFE LSLIEARGLN QNYISPEHIL LALIREPEGV
     AYTILGNLGV DFSKLRNEII NNIAGDETQQ GSSPKKGKSS TPTLEKYGKD LTELAKEGKL
     DPIIGRDKET ERVLEILCRR IKNNPCLIGD PGVGKTAIAE GLAQKIATGN IPELLKDKRV
     VTLDLSSMVA GSKYRGEFEE RLKSVMDEIS KAGDVILFID EIHTIVGAGG AEGAIDASNI
     LKPALGRGEI QCIGATTLEE YRKYIEKDAA LERRFQPVTV EEPTKEEAVE ILKGLRDKYE
     AHHRVKITDD AILAAVNLSD RYITDRYLPD KAIDLIDEAG SKVRIQNLTA PKDLKELEND
     LEVVIKEKAD AITMQDFEKA ATLRDKEKEL KDKLEDSKKN WVSQNNGADA VVDEKHIANV
     ISKWMSIPIE KLTESEAERL LKLEEILHKR VIGQEEAVES IARAVRRARV GLKDPKRPIG
     SFIFLGPTGV GKTELSKALA EAMFGDEKSI IRVDMSEYME RHTVSKLIGA PPGYVGFDDG
     GQLTERIRRH PYSVVLFDEI EKAHPDVFNI LLQILEDGRL TDGKGKTVDF KNTIVIMTSN
     AGASTIRKQK TIGFSQSVNE ANNEHEKMKE NIMEELKRSF RPEFLNRIDD IIVFHSLAEE
     DLLEIVGLML NSVSERLKEK EINIKFDEES KKYLAKEGFD PTYGARPLRR AITKTVEDKL
     SEEILKGNVK QGDSLIVTVE ENELKFNKQ
//
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