ID A0A0R1JZI7_9LACO Unreviewed; 467 AA.
AC A0A0R1JZI7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=ATP-dependent protease ATP-binding subunit HslU {ECO:0000313|EMBL:KRK73322.1};
GN ORFNames=FD02_GL001180 {ECO:0000313|EMBL:KRK73322.1};
OS Lacticaseibacillus nasuensis JCM 17158.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1291734 {ECO:0000313|EMBL:KRK73322.1, ECO:0000313|Proteomes:UP000051804};
RN [1] {ECO:0000313|EMBL:KRK73322.1, ECO:0000313|Proteomes:UP000051804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17158 {ECO:0000313|EMBL:KRK73322.1,
RC ECO:0000313|Proteomes:UP000051804};
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:KRK73322.1}.
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DR EMBL; AZDJ01000013; KRK73322.1; -; Genomic_DNA.
DR RefSeq; WP_056950619.1; NZ_AZDJ01000013.1.
DR AlphaFoldDB; A0A0R1JZI7; -.
DR STRING; 1291734.FD02_GL001180; -.
DR PATRIC; fig|1291734.4.peg.1211; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000051804; 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:KRK73322.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:KRK73322.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KRK73322.1};
KW Protease {ECO:0000313|EMBL:KRK73322.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051804}.
FT DOMAIN 48..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; 51608 MW; DAEEE1C3E6424EAA CRC64;
MVQTPKEIVA QLDQYVIGQT DAKRAVAVAL YNRWRRLQLS PKMQQDITPK NLLMIGPTGV
GKTEIARRLA KIVKAPFVKV EATKFTEVGY VGRDVESMVR DLAEVAVSMA EADAFAKVRT
RATREANKRL VKLLVPAIKK EKRASNNPMG DMMKLFQNMQ NGEAPQPDQD EGEITESIKS
ERLSVADQLE AGLLEDRELT VAVADEKKPG GLGDMYGQMG IDLSDTLGNL MPKQKVQRTM
TVREAREIFI REESDKLVNH ADIYHEAIAA AENNGIIFID EIDKIAAGNK NTSGEVSREG
VQRDILPIVE GAQVSTKYGP LNTDHVLFIG SGAFATAKPS DLIPELQGRF PIRVELNDLT
EADFVRILTE PDNALVKQYI ALIGADGVHV TFTKEAIEQI AKIATRVNRD TDNIGARRLA
TILEKLLEDV LYEGPDMQMG DITVTAKYVD DKIGHIAADA DQTRYIL
//