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Database: UniProt
Entry: A0A559QN02_9ALTE
LinkDB: A0A559QN02_9ALTE
Original site: A0A559QN02_9ALTE 
ID   A0A559QN02_9ALTE        Unreviewed;       765 AA.
AC   A0A559QN02;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:TVZ39194.1};
GN   ORFNames=P886_3589 {ECO:0000313|EMBL:TVZ39194.1};
OS   Alteromonadaceae bacterium 2753L.S.0a.02.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae.
OX   NCBI_TaxID=1403320 {ECO:0000313|EMBL:TVZ39194.1, ECO:0000313|Proteomes:UP000318527};
RN   [1] {ECO:0000313|EMBL:TVZ39194.1, ECO:0000313|Proteomes:UP000318527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2753L.S.0a.02 {ECO:0000313|EMBL:TVZ39194.1,
RC   ECO:0000313|Proteomes:UP000318527};
RA   Haygood M.;
RT   "Genome sequencing of Philippine Mollusk Symbiont ICBG bacterial isolates
RT   from shipworm (Teredinidae) gill.";
RL   Submitted (JUN-2019) 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:TVZ39194.1}.
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DR   EMBL; VISH01000002; TVZ39194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A559QN02; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000318527; 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:TVZ39194.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TVZ39194.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000318527};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          145..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  84425 MW;  1DE7F03C8B4B16B3 CRC64;
     MLSKELEATL NNAFKGARSK RHEFMTVEHL LLALLDNESA ASVLRACGAD LGILRRDLAE
     FVDSTTPLIP EDDKERETQP TLGFQRVLQR AVFHVQSSGK SEVTGANVLV AIFSEQESQA
     VYYLKQQSIA RIDVVNFITH GISKVSGSNS HSDSGSEQMD DEVSAGGDSS QQNPLESYAT
     NLNEQAMKGR IDPLVGREFE VERVVQILAR RRKNNPLLVG ESGVGKTAIA EGLAKKIIDN
     EVPEVLENST VYSLDLGSLL AGTKYRGDFE KRFKGLLAEL KKREHAILFI DEIHTIIGAG
     AASGGVMDAS NLLKPLLTSG DLRCIGSTTF QEYRGIFDKD RALSRRFQKI DVNEPSVEDT
     YKILRGLKSR FEKHHNLKYT DTALKTAAEL ASKYISDRYM PDKAIDVIDE AGAYQQLLPE
     SKRKKIIGVR DIENIIAKIA RVPAKTVSSN DKELLSKLED TLRMTVFGQE EAITAISSAI
     KLSRAGLTNH EKPIGSFLFA GPTGVGKTEL CKQLASAMGV ELVRFDMSEY MERHTVSRLI
     GAPPGYVGFD QGGLLTDAVT KQPHSVVLLD EIEKAHPDVF NLLLQVMDHG ALTDNNGRSA
     DFRNVVLIMT TNAGAETMSR ASIGFTKQDH SSDGMEAIKR AFTPEFRNRL DGIIQFGSLS
     LEVVKTVVDK FLMELQAQLD DKKITMEVTD EARDWLAVHG YDEKMGARPM ARIIQESVKK
     PLAEMVLFGE LADRGGVVTV LVEEDKLKVV AQPETYEERT PEMCT
//
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