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Database: UniProt
Entry: Q2SB15_HAHCH
LinkDB: Q2SB15_HAHCH
Original site: Q2SB15_HAHCH 
ID   Q2SB15_HAHCH            Unreviewed;      1101 AA.
AC   Q2SB15;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:ABC32159.1};
GN   Name=clpC {ECO:0000313|EMBL:ABC32159.1};
GN   OrderedLocusNames=HCH_05497 {ECO:0000313|EMBL:ABC32159.1};
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC32159.1, ECO:0000313|Proteomes:UP000000238};
RN   [1] {ECO:0000313|EMBL:ABC32159.1, ECO:0000313|Proteomes:UP000000238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC32159.1,
RC   ECO:0000313|Proteomes:UP000000238};
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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DR   EMBL; CP000155; ABC32159.1; -; Genomic_DNA.
DR   RefSeq; WP_011399222.1; NC_007645.1.
DR   AlphaFoldDB; Q2SB15; -.
DR   STRING; 349521.HCH_05497; -.
DR   KEGG; hch:HCH_05497; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_288168_0_0_6; -.
DR   OrthoDB; 1488255at2; -.
DR   Proteomes; UP000000238; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 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; IPR011704; ATPase_dyneun-rel_AAA.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF07728; AAA_5; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ABC32159.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000238}.
FT   DOMAIN          220..356
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          491..643
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          657..748
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          1079..1101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1101 AA;  126010 MW;  B22A9F16DD19AEA2 CRC64;
     MSKQFSFPFY NTILTHESGV TLTLPGNMTE IAWLNAPSAH VARQFQKRAQ RKLLKQGEYV
     ELLHYLPEGE TEVREVKVKV PASREGGYTG HEITFEAVIW RLRQGEILGV VPALAVACLC
     WDEEQIMQRV SECIQLEMLR NKRFGSARSL IACQWYAPPK VVREEVMLEF YTPAELADLR
     RQQDEPVIAK TARRMHRSRA SVFGLDAYVD TLNRNLLGEF RQSVLVVGPS GCGKTALINE
     FVKRHFTGVN SNKIPWRTTA AQMLQALTQQ GGWRHALGLW VREARTNGEI IYLGNLSELF
     EVGQYQGNSV SIAEALRDPL SRNEVTLIAE VTEEQLAAID LRAPGYSQLF HIVRFTERGE
     EEENQIARQA IQAQADLFNI RIAPNAIERI ILLQRRYAPY SGYPGKIIRF FENMILAARK
     DNGAISENEA ISASCEESGM PRFLVDHQAR LDADKVREHF RRRIVGQTQA VEALVRAIIT
     VKAGLAPRGK PIASLLFVGP TGVGKTEMAK TLAQFMFGDE KRLLRFDMSE YSDPYSVTRL
     TATGEASLVT KVRQQPFSVL LFDEIEKADP AFYDLLLQVL GEGRLTDDHG ESANFCSALI
     IMTSNLGAQQ FMQNSVGFST EDKTDAAAQR HFEQTAAKYF RPELFNRIDQ VAPFFALTQA
     EQMIVLQKEM RRLQGAAGLS NRQVSLNFED PVWSHLNNLP SDPRYGARSV QRLLRKHVTA
     HLAPALSARP HEDPLEITAT VSADALSFDA RVTHQEKRAR GYFMELTEKV AAHRRDLQAL
     QESPTWISCL SELDQMDARK RRKRNSFWED PEQTRRYGEL FNLREALTQR IDDAYALENE
     CLGQLLDQHS AMRAEDYEEA LRELQTRFDD FLIEIESTLN PHYNRHLLFV YGGQPQLDRL
     SLWYERWFEK LDHDYTRVWI YLDPDLDANP ITEAVPHGEF VELVTLPPYK VSKDMLTQEE
     LPLIGMGWVL SGACVQYFWR HDHGKVDWAT EEDKNAPMYI DFNDAKLDEY EVPAGIHRMK
     FYKDMKAHRK VREEEYQDER FGDPQTYQDL FGHSERVKHK AARSLQEKLL ARLVIRQEKK
     PEDKKRGAKS AYDDAAGGLQ E
//
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