ID A0A377PWG0_9HELI Unreviewed; 848 AA.
AC A0A377PWG0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574};
GN Name=clpB {ECO:0000313|EMBL:STQ86774.1};
GN ORFNames=LS73_007025 {ECO:0000313|EMBL:TLD99614.1}, NCTC12714_01585
GN {ECO:0000313|EMBL:STQ86774.1};
OS Helicobacter muridarum.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=216 {ECO:0000313|EMBL:STQ86774.1, ECO:0000313|Proteomes:UP000255139};
RN [1] {ECO:0000313|EMBL:TLD99614.1, ECO:0000313|Proteomes:UP000029922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST1 {ECO:0000313|EMBL:TLD99614.1,
RC ECO:0000313|Proteomes:UP000029922};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
RN [2] {ECO:0000313|EMBL:STQ86774.1, ECO:0000313|Proteomes:UP000255139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12714 {ECO:0000313|EMBL:STQ86774.1,
RC ECO:0000313|Proteomes:UP000255139};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UGJE01000002; STQ86774.1; -; Genomic_DNA.
DR EMBL; JRPD02000016; TLD99614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377PWG0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000029922; Unassembled WGS sequence.
DR Proteomes; UP000255139; 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: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 Gene3D; 4.10.860.10; UVR domain; 1.
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; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
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; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:STQ86774.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:STQ86774.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:STQ86774.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000255139};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 201..346
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 587..751
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 750..839
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 428..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 94352 MW; 6C996F556893C667 CRC64;
MGSTSKINEN LGFILQKALG LVEELHQDIM TVEHVFYSLL EHPLGGEMVM AIGGNVPNLM
ESTVTYLDKY IPKAKQLKQL EGPSQTLAFS RVFDQMIIHA QSANKSIIGI GDFLVALMKE
TDCYASQLLR SQGIEIDDVM RIAVEFDEDK REREKHSKGS LSNLEKYAKN LNKIAKEGKI
DPLIGREYEI NQIAQVLCRR KKNNPILLGE AGVGKSAIVE GLALRIVEGN VPKKLLDSVI
YAIDVSSVIA GTKYRGEFET RIKKILAEIE NDENTIIFFD EIHMIVGAGQ SHNGSMDFSN
LLKPMLSSGK LRCIGATTIS EYKTSFDKDK ALARRFTQIK IDEPSEEECL KIIQKIAPIY
ERFHNVTYEE DALKACVTLS AKYISEKHLP DKAIDLLDEA GAKAQLNEYT LKQQINLSQT
FMSGVKNDAK DASNARSSND DLPSKSDFEL DREQSSDGIA NGLSKDYALT PLELKEIDSE
KKQDSKIYRY EPVKGIVGNS AKAESNHKPQ IDFMKNTHKV ITQNHIELLM SDITNIPKST
INANESSLLK NLDKLLKKRI FSQDAAIEKI VEKITINKAG LSELNRPIAS FLFTGPSGVG
KTELSKELAR ILGIKFERID MSEYMEPHSI SKLIGSPAGY VGYDEGGLLV NKIRVNPHCV
LLLDEIEKAH SDVYNILLQI MDSATLTDNQ NNKADFKNVI LIMTTNAGSK EGNSMGFLDT
TPNRSDKAIK DTFSPEFRSR LDAVIVFKQL GIYDMQRIAD KYISDLNATL KERCVTLKLL
PKAAKFIAQS SIDAALGARE IKKIIDSVIK LPLGKEILFG KLRKGGAVNI TVKKNELALE
IIEDKVLV
//