ID A0A0R2N3E8_9LACO Unreviewed; 467 AA.
AC A0A0R2N3E8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=ATP-dependent protease ATP-binding subunit HslU {ECO:0000313|EMBL:KRO18259.1};
GN ORFNames=IV56_GL001390 {ECO:0000313|EMBL:KRO18259.1};
OS Lacticaseibacillus saniviri JCM 17471 = DSM 24301.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1293598 {ECO:0000313|EMBL:KRO18259.1, ECO:0000313|Proteomes:UP000050969};
RN [1] {ECO:0000313|EMBL:KRO18259.1, ECO:0000313|Proteomes:UP000050969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24301 {ECO:0000313|EMBL:KRO18259.1,
RC ECO:0000313|Proteomes:UP000050969};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRO18259.1}.
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DR EMBL; JQCE01000005; KRO18259.1; -; Genomic_DNA.
DR RefSeq; WP_054776449.1; NZ_JQCE01000005.1.
DR AlphaFoldDB; A0A0R2N3E8; -.
DR STRING; 1293598.IV56_GL001390; -.
DR PATRIC; fig|1293598.4.peg.1455; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000050969; 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 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:KRO18259.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:KRO18259.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KRO18259.1};
KW Protease {ECO:0000313|EMBL:KRO18259.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050969}.
FT DOMAIN 50..356
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 359..458
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 467 AA; 52021 MW; A831968181A56C89 CRC64;
MSDVKTPKEI VAQLDQYVIG QSDAKRAVAV ALYNRYRRMQ LSDKLQREIT PKNLLMIGPT
GVGKTEIARR LARIVNAPFV KVEATKFTEV GYVGRDVESM VRDLADVAVQ MEEDRQFANV
HGRAEREANK RLVKLLVPGI KKEKRTNPMN DVMSMLQGLQ NGQAPEAESD DGEITDDIRN
ERLSVAEQLE KGLLEDRELT VTVADEKKGN GMNDMYGQMG IDLSESLGAL MPKQRVERTM
TVKEAREVFT REESDKLVNH ADIYHDAIKA AENNGIIFID EIDKIAAGNK KTSGEVSREG
VQRDILPIVE GSQVNTKYGP LSTDHVLFIG SGAFAESKPS DLIAELQGRF PIRVELNDLN
EADFVSILTE PDNALVKQYM ALIGTDGVQV TFTQEAIQSI AHIAMQVNHD TDNIGARRLA
TILEKLLEDI LYEGPDMQMG SITITEQYVD DKIGQIVADK DMTRYIL
//