ID B6BIR0_SULGG Unreviewed; 859 AA.
AC B6BIR0; H1FW36;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574};
GN Name=clpB {ECO:0000313|EMBL:EHP30418.1};
GN ORFNames=SMGD1_1895 {ECO:0000313|EMBL:EHP30418.1};
OS Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP30418.1, ECO:0000313|Proteomes:UP000006431};
RN [1] {ECO:0000313|EMBL:EHP30418.1, ECO:0000313|Proteomes:UP000006431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD1 {ECO:0000313|EMBL:EHP30418.1,
RC ECO:0000313|Proteomes:UP000006431};
RX PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA Labrenz M., Jurgens K.;
RT "Genome and physiology of a model Epsilonproteobacterium responsible for
RT sulfide detoxification in marine oxygen depletion zones.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
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:EHP30418.1}.
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DR EMBL; AFRZ01000001; EHP30418.1; -; Genomic_DNA.
DR RefSeq; WP_008335124.1; NZ_DS995286.1.
DR AlphaFoldDB; B6BIR0; -.
DR STRING; 929558.SMGD1_1895; -.
DR PATRIC; fig|929558.5.peg.1890; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000006431; 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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; -; 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; 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 PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 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.
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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:EHP30418.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EHP30418.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006431};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 6..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 859 AA; 95357 MW; B8F102FB8D51F831 CRC64;
MNNNIFEKLT HNMTEAIESS ISLALHNKNQ EVGSIHFLWA LLTNSNSVLN QMFNKMNIDK
VAIELDVKSL SEKLPKSSTV SKENIKLSRD FVHTLENGAG LMTKNGDSFL AVDTYILANL
KDEPYSSILK KYIDVLELAK NLEAARAGAK IQTQSSDETL ESLDKYGIDL TAEAREGKLS
PVIGRDEEIT RMMQILIRKT KNNPMLLGEP GVGKTALVEG LAQRISDNKV PTSLKNKRLV
ALDMSALIAG AKYRGEFEDR LKAVIDEVKK SGNIILFIDE IHTIVGAGAS EGSMDAANIL
KPALARGELH TIGATTLKEY RKYFEKDMAL QRRFLPINLD EPTVNQSLQI LRGIKGRLET
HHNVTITDSA LVAAAKLSDR YIADRFLPDK AIDLIDEAAA ELKMQIESEP NVLGSAKRKS
SELQVEKEAL KMEKTPANEK RLGEIEKELA NVEEEVRSLE AQFASEKEVF ERISGIKNDI
EKKRKEAHAA KSNSEFNRAA EIEYGEIPAL LEEEKSINAN WEKLQLAGTL LKNSVDEEAI
ASIVSRWTNI PVTKMLQGDK DKILNVEAEL NRDVIGQAKA THAVSRAIKR NKAGLSDANT
PIGSFLFLGP TGVGKTQTAK TLAKFLFDSE DSMIRIDMSE YMEKHAVSRL VGAAPGYVGY
EEGGQLTEAV RRKPYSVILF DEVEKAHPDV FNILLQVLDD GRLTDNKGVT VDFSNTIIIL
TSNIASDKII NNPASDELDN MVLSELKQAF KPEFLNRLDD IVIFNALGRE QIIDIVDIFF
SDISRKVEQR DIELTLSDSA KAYIAEAGFD PVYGARPLKR ALYEIVEDRL AELILEGKVM
EGSKVLFDIE NGEIKVSVK
//
