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Database: UniProt
Entry: A0A4Q9XS59_9ALTE
LinkDB: A0A4Q9XS59_9ALTE
Original site: A0A4Q9XS59_9ALTE 
ID   A0A4Q9XS59_9ALTE        Unreviewed;       754 AA.
AC   A0A4Q9XS59;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, entry version 14.
DE   SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:TBX27467.1};
GN   Name=clpA {ECO:0000313|EMBL:TBX27467.1};
GN   ORFNames=TK45_01640 {ECO:0000313|EMBL:TBX27467.1};
OS   Bowmanella sp. JS7-9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Bowmanella.
OX   NCBI_TaxID=1605368 {ECO:0000313|EMBL:TBX27467.1, ECO:0000313|Proteomes:UP000291390};
RN   [1] {ECO:0000313|EMBL:TBX27467.1, ECO:0000313|Proteomes:UP000291390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS7-9 {ECO:0000313|EMBL:TBX27467.1,
RC   ECO:0000313|Proteomes:UP000291390};
RA   Dong C., Shao Z.;
RT   "High-quality draft genome sequence of Bowmanella sp. JS7-9.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:TBX27467.1}.
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DR   EMBL; JXSY01000002; TBX27467.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q9XS59; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000291390; 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:0043335; P:protein unfolding; IEA:InterPro.
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; IPR013461; ClpA.
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   NCBIfam; TIGR02639; ClpA; 1.
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:TBX27467.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TBX27467.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291390};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          144..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   754 AA;  83779 MW;  403DBFD399E59E07 CRC64;
     MLNKDLERTL NEAFIFAREH RHEFMTVEHL LLALLNNPSA AEALRACGAD IPAIKRELED
     FVKDTTPILL EDETGERETQ PTLGFQRVLQ RAVFHVQSSG KDEVTGANVL VAIFSEQESQ
     AVYILKKSDV TRLDVVNFIS HGVTKSEDER PAQHETESEA GEGEDRSAML ERFSTNLNEL
     AAKGKIDPLI GRDAELERTV QILCRRRKNN PLLVGEAGVG KTAIAEGLAY RIVNNQVPDV
     IANATVYSLD LGGLLAGTKY RGDFEKRLKA ILKELEKQPE AILFIDEIHT IIGAGAASGG
     VMDASNLLKP KLSSGELRCI GSTTYQEYQG IFEKDRALAR RFQKIDVTEP SVEDTTRILM
     GLKDRYEKHH DVKFTKQAMR AAAELAAKYI NERHLPDKAI DVIDEAGASQ RLLPVSKRKK
     TIGVTDIEQI IAKIARIPEK SVSASDKEVL KNLDRNLKMV VFGQDKAIES LTDAIRLSRS
     GLGNEKKPVG CFLFAGPTGV GKTEVTQQLA KIMGVELTRL DMSEYMERHA VSRLIGAPPG
     YVGFDQGGLL TDAVIKHPYS VVLLDEIEKA HSDIYNILLQ VMDHGTLTDN NGRKVDFRNV
     VLVMTTNAGV QQTQRKSIGF QQQDHSHDAL SEINKIFSPE FRNRLDGIIW FNHLDAQIIL
     QVVDKFIVEL EAQLDAKSVS LEVTPAARAW LAEKGYDKAM GARPMSRLIQ EKVKKELANE
     LLFGKLTKGG SVVVDEQDDN LTFNYTQVAE HEKA
//
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