ID A0A1B8J6L4_9HELI Unreviewed; 462 AA.
AC A0A1B8J6L4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=HslU--HslV peptidase ATPase subunit {ECO:0000313|EMBL:OBV28585.1};
GN ORFNames=BA723_08870 {ECO:0000313|EMBL:OBV28585.1}, BKN38_08255
GN {ECO:0000313|EMBL:OHU81798.1};
OS Helicobacter sp. CLO-3.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=211 {ECO:0000313|EMBL:OBV28585.1, ECO:0000313|Proteomes:UP000092701};
RN [1] {ECO:0000313|EMBL:OBV28585.1, ECO:0000313|Proteomes:UP000092701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMC1 {ECO:0000313|EMBL:OBV28585.1,
RC ECO:0000313|Proteomes:UP000092701};
RA Greninger A.L., Bateman A., Jerome K., Fang F.;
RT "Genome sequence of Helicobacter sp. CLO-3.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OHU81798.1, ECO:0000313|Proteomes:UP000179541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLO-3 {ECO:0000313|EMBL:OHU81798.1,
RC ECO:0000313|Proteomes:UP000179541};
RA Greninger A.L., Bateman A.C., Fang F., Jerome K.;
RT "Genome sequence of Helicobacter sp. CLO-3 Fennel-37 strain.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OBV28585.1}.
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DR EMBL; MAMQ01000107; OBV28585.1; -; Genomic_DNA.
DR EMBL; MLQN01000032; OHU81798.1; -; Genomic_DNA.
DR RefSeq; WP_066457911.1; NZ_MLQN01000032.1.
DR AlphaFoldDB; A0A1B8J6L4; -.
DR STRING; 211.BKN38_08255; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000092701; Unassembled WGS sequence.
DR Proteomes; UP000179541; Unassembled WGS sequence.
DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
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 Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000092701}.
FT DOMAIN 46..325
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 328..428
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 462 AA; 51811 MW; F2210739232212DA CRC64;
MTPREIVAFL DEYIIGQNDA KRAIAIALRN RYRRIQLPQE IQEEITPKNI LMIGSTGVGK
TEIARRMAKI MGLPFIKVEA SKYTEVGFVG RDVESMIRDL VSVSIALVQS EHQEKSAQDI
QKYIIDKIAS ILLPPLPSSV SEDKKKEYQI SLEKMRQKVQ NGEMDHLQIE LEIAKKMESF
DNNMPPEMIK VQESIIKVLN HQEKIKKSLS VKEAKIALAQ EAKDAVLDME SIRAEGLKRA
ESSGVVFIDE IDKIATSSKD SRLDPSKEGV QRDLLPIIEG SSINTKYGAI KTDYILFVAA
GAFHLSKPSD LIPELQGRFP IRVELDSLDE ESMYKILTQT RTSLIRQYQH LLGVEGVELV
FEEEALRVLA HFAYMANQKT QDIGARRLHT ILERVLEDIS FDAQEFVKNA RADSGVDSAS
GADSGARVDS NGGKNKVVIE KSLIEEKLSN LVSNADITRY IL
//
