ID A0A4V6I6P6_9HELI Unreviewed; 445 AA.
AC A0A4V6I6P6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=HslU--HslV peptidase ATPase subunit {ECO:0000313|EMBL:TLE16328.1};
GN Name=hslU {ECO:0000313|EMBL:TLE16328.1};
GN ORFNames=LS72_003455 {ECO:0000313|EMBL:TLE16328.1};
OS Helicobacter apodemus.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=135569 {ECO:0000313|EMBL:TLE16328.1, ECO:0000313|Proteomes:UP000029920};
RN [1] {ECO:0000313|EMBL:TLE16328.1, ECO:0000313|Proteomes:UP000029920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT-03-7007 {ECO:0000313|EMBL:TLE16328.1,
RC ECO:0000313|Proteomes:UP000029920};
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).
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:TLE16328.1}.
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DR EMBL; JRPC02000007; TLE16328.1; -; Genomic_DNA.
DR RefSeq; WP_034552545.1; NZ_JRPC02000007.1.
DR AlphaFoldDB; A0A4V6I6P6; -.
DR Proteomes; UP000029920; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000029920}.
FT DOMAIN 52..338
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 337..436
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 144..171
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 445 AA; 50423 MW; 13C695FCED17AFAC CRC64;
MEKFANLTPK EIVAYLDEYI IGQNEAKKVV AIALRNRYRR LKLPKEIQDE IMPKNILMMG
STGVGKTEIA RRMAKIMGLP FIKVEASKYT EVGFVGRDVE SMVRDLVIAS INLVKEEYRL
KNAEDIEKYV LDKIVQKLIP PLPKGASEQK IEEYEKTASK MKMRVEKGEM DSLKIEIETP
KRSLEIDDSN MPAEFIKVQE TIAKVFVTSK ENPRKEVTIK EAKEILKIEA SEALLDMESI
KQEGLKRAES SGIIFIDEID KVAVSSKSQG RQDPSKEGVQ RDLLPIVEGS VVNTKYGSIK
TDHILFIAAG AFSLSKPSDL IAELQGRFPL RVELDSLDEE ALYKILTQTK NSILRQYEAL
LGVEEVTLKF DEEAIRALAY YSQKANEKTE DIGARRLHTV VEQVLEDISF KAEKYQGEVV
SITKELVKEK LEEIVANVDM ARYIL
//