GenomeNet

Database: UniProt
Entry: A0A4S4BV89_9BACL
LinkDB: A0A4S4BV89_9BACL
Original site: A0A4S4BV89_9BACL 
ID   A0A4S4BV89_9BACL        Unreviewed;       815 AA.
AC   A0A4S4BV89;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:THF79061.1};
GN   ORFNames=E6C55_12650 {ECO:0000313|EMBL:THF79061.1};
OS   Cohnella fermenti.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2565925 {ECO:0000313|EMBL:THF79061.1, ECO:0000313|Proteomes:UP000310636};
RN   [1] {ECO:0000313|EMBL:THF79061.1, ECO:0000313|Proteomes:UP000310636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-MHH1044 {ECO:0000313|EMBL:THF79061.1,
RC   ECO:0000313|Proteomes:UP000310636};
RA   Lin S.-Y., Hung M.-H., Young C.-C.;
RT   "Cohnella sp. nov. isolated from preserved vegetables.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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:THF79061.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; SSOB01000014; THF79061.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S4BV89; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000310636; 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: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   Hydrolase {ECO:0000313|EMBL:THF79061.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:THF79061.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000310636};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          417..452
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          453..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   815 AA;  90607 MW;  CAB86BF6D50E3A33 CRC64;
     MMFGRFTERA QKVLALAQEE AVRLGHNNIG TEHILLGLIR EGESIAAKAL IALGLGLEKI
     QDEVESLIGR GQEQPTNIAY TPRAKKVIEL SMDEARKLGH TYVGTEHILL GLIREGEGVA
     ARVLNNLGIS LNKARQQVLQ LLGSSESVSP SHGPSANVST PTLDGLARDL TASARDNNID
     PVIGRAKEIE RVIQVLSRRT KNNPVLIGEP GVGKTAIAEG LAQKIVNNEI PETLRDKRVM
     TLDMGSVVAG TKYRGEFEDR LKKIMDEIRQ AGNVILFIDE LHTLIGAGGA EGAIDASNIL
     KPALARGELQ CIGATTLDEY RKYIEKDAAL ERRFQPITVD QPSPEEAVQI LHGLRDRYEA
     HHRVKITDDS IEAAVKLSDR YITDRFLPDK AIDLIDEASS KVRLRSYTIP PNLKQLEQRL
     EDIRKEKDAS VQSQEFEKAA ALRDTEQKIR EELDATKNQW KEKQGRTDSE VTPEDIAQVV
     ASWTGIPVSK LAEEETERLL KMEEILHDRV IGQEEAVKAV ARAVRRSRAG LKDPKRPIGS
     FIFLGPTGVG KTELARALAE AMFGDENAVI RIDMSEYMEK HSTSRLVGAP PGYVGYDEGG
     QLTEKVRRKP YSVVLLDEIE KAHPEVFNVL LQVLEDGRLT DSKGRTVDFR NTLIIMTSNV
     GADQIKRNST LGFTAAHDAG RDYAVMKDKV LGELKKSFRP EFLNRIDEMI VFHPLEQEHI
     ARIVTLMADE LRKRLAEHDV EFELTEAAKA FLAKEGFDPQ YGARPLRRAI QKHIEDRLSE
     ELLLGKIQKG HKLLIDEADG TLAVQVKDEV GSTNL
//
DBGET integrated database retrieval system