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Database: UniProt
Entry: E7G4L3_9HELI
LinkDB: E7G4L3_9HELI
Original site: E7G4L3_9HELI 
ID   E7G4L3_9HELI            Unreviewed;       446 AA.
AC   E7G4L3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=ATP-dependent protease, ATP-binding subunit {ECO:0000313|EMBL:EFX41706.1};
GN   Name=hslU {ECO:0000313|EMBL:EFX41706.1};
GN   ORFNames=HSUHS5_0924 {ECO:0000313|EMBL:EFX41706.1};
OS   Helicobacter suis HS5.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=710394 {ECO:0000313|EMBL:EFX41706.1, ECO:0000313|Proteomes:UP000054093};
RN   [1] {ECO:0000313|EMBL:EFX41706.1, ECO:0000313|Proteomes:UP000054093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS5 {ECO:0000313|EMBL:EFX41706.1,
RC   ECO:0000313|Proteomes:UP000054093};
RX   PubMed=21414191; DOI=10.1186/1297-9716-42-51;
RA   Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A.,
RA   De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.;
RT   "Genome sequence of Helicobacter suis supports its role in gastric
RT   pathology.";
RL   Vet. Res. 42:51-51(2011).
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000256|ARBA:ARBA00009771}.
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:EFX41706.1}.
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DR   EMBL; ADHO01000173; EFX41706.1; -; Genomic_DNA.
DR   RefSeq; WP_006564227.1; NZ_ADHO01000173.1.
DR   AlphaFoldDB; E7G4L3; -.
DR   GeneID; 56927942; -.
DR   Proteomes; UP000054093; Unassembled WGS sequence.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
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; cd19498; RecA-like_HslU; 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; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004491; HslU.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00390; hslU; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000313|EMBL:EFX41706.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:EFX41706.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:EFX41706.1};
KW   Protease {ECO:0000313|EMBL:EFX41706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054093}.
FT   DOMAIN          54..335
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          338..432
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   446 AA;  50422 MW;  3CCD9155E304E5DD CRC64;
     MVGHAKLNLT PQEIVRYLDD YIIGQQDAKK MIAIALRNRW RRLQLSKELQ EEVMPKNILM
     IGSTGVGKTE IARRMAKMMG LPFIKVEASK YTEVGFVGRD VESMVRDLVV ASIHLVENEE
     KEKNQAKIED LIIERITKKL LPPLPSGVGK DKQQEYALNF EKTKQKVRSH VLDDQKIQIE
     LDKRGVEGDF NMPPEIIKVQ ESLTKILNKG GEKVSKEMTI KEAKEALRHD VSQAILDMEQ
     VQREGVQRAA QCGVIFIDEI DKIAVGSKEG RTQDPSKEGV QRDLLPIVEG STIQTKYGPI
     ATDHILFIAA GAFHLSKPSD LIPELQGRFP LRVELESLSE EIMYEILTRP KSSLIKQYQA
     LLEVENVDLA FEPEALRELA RFSYLANQKT EDIGARRLHT TLEKVLEDIS FNATAYAGQK
     VVVSKKDVSQ TLQDLVEDVD LARFIL
//
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