ID Q21KI1_SACD2 Unreviewed; 897 AA.
AC Q21KI1;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 24-JAN-2024, entry version 106.
DE SubName: Full=ATPase AAA-2 {ECO:0000313|EMBL:ABD80798.1};
GN OrderedLocusNames=Sde_1536 {ECO:0000313|EMBL:ABD80798.1};
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD80798.1, ECO:0000313|Proteomes:UP000001947};
RN [1] {ECO:0000313|EMBL:ABD80798.1, ECO:0000313|Proteomes:UP000001947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024
RC {ECO:0000313|Proteomes:UP000001947};
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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; CP000282; ABD80798.1; -; Genomic_DNA.
DR AlphaFoldDB; Q21KI1; -.
DR STRING; 203122.Sde_1536; -.
DR KEGG; sde:Sde_1536; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_1_0_6; -.
DR OMA; YGGERKM; -.
DR Proteomes; UP000001947; Chromosome.
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; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017729; ATPase_T6SS_ClpV1.
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; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03345; VI_ClpV1; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001947};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 14..165
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 897 AA; 99440 MW; 517AE405B5EEF7E5 CRC64;
MTLLDNLKEM TMEFEKLVKN LSNESKELFE KSIALASSRS HFYIDVEHWL TEALAEEQRE
IIAILKHFNV DVDRVHADLD LALENTKTGN DGFPKISPDI VRLLFEAWMI ASSQYASVQV
LPVHILLALV DSAGLKTKIG KISKQFEAIS GEEIRTQCET LLRGEALQDQ GEATNKKLTK
TPSLDQFTTN LTQQAKDGKI DSILGRDDEI RQIIDVLCRR KQNNPILTGE AGVGKTAVVE
GLAVKIAQGD VPTAIENVEI RSLDLGLLQA GAGVKGEFEN RLKNVIKEVQ QSVQSIILFI
DEAHTLIGAG NQAGSGDAAN LLKPALARGE LRTIAATTWA EYKKYFESDA ALTRRFQVVK
VEEPSVDKAI IMLRNAAPTL EQHHKVVILD AAVSASVNLS HRYIPGRQLP DKCVSLLDTA
CARVNLSQNT TPARIVQYSQ EIKNIEFEIE RLNQEAEKGY EHSASIVELE VKKVGITERY
QSLCARWEQE KQIINQINSA REKAEEKVQD SDNEESATDL TNTLIAELRV KLKSISGSQP
LIYECVDEQV VAEVVADWTG IPVGRMQSDE IQNVLSLEQT MEKRVIGQSH GLKLISKAVQ
TARAKLSDPK RPLGVFMLVG PSGVGKTETA LTLAEQLYGS EQNMTVINMS EFKEEHKVSM
LMGSPPGYVG YGEGGVLTEA VRRKPYSVVL LDEMEKAHPG VQDIFYQVFD KGILRDGEGR
DIDFKNTVII MTSNTASAQI EQLCIDPETK PEPKALLEAI EGTLRETYKP AFLGRINLIP
YYPLDEQCLS EIAVMQLHAI QQRVETNYKV ELNYSDKLVE HVVSLCAQSD TGARKISALL
NNTLLPVLAE KILTEIALDK ALESVEVDVS EEGEFVVKIN SKKENTDDMK IKKTVTG
//