ID A0A1S6QJA5_9LACO Unreviewed; 749 AA.
AC A0A1S6QJA5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:AQW21685.1};
GN ORFNames=PL11_006980 {ECO:0000313|EMBL:AQW21685.1};
OS Lentilactobacillus curieae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1138822 {ECO:0000313|EMBL:AQW21685.1, ECO:0000313|Proteomes:UP000030361};
RN [1] {ECO:0000313|EMBL:AQW21685.1, ECO:0000313|Proteomes:UP000030361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC M 2011381 {ECO:0000313|EMBL:AQW21685.1,
RC ECO:0000313|Proteomes:UP000030361};
RX PubMed=26021929;
RA Wang Y., Wang Y., Lang C., Wei D., Xu P., Xie J.;
RT "Genome Sequence of Lactobacillus curieae CCTCC M 2011381T, a Novel
RT Producer of Gamma-aminobutyric Acid.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP018906; AQW21685.1; -; Genomic_DNA.
DR RefSeq; WP_035168316.1; NZ_CP018906.1.
DR AlphaFoldDB; A0A1S6QJA5; -.
DR KEGG; lcu:PL11_006980; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000030361; Chromosome.
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; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR036876; UVR_dom_sf.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS50151; UVR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:AQW21685.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:AQW21685.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:AQW21685.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030361}.
FT DOMAIN 356..391
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 65..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 82827 MW; CF50E8A802570AC1 CRC64;
MLCQNCHQNE ATIHLYTNVN GSKQTINLCQ NCYQLLTNRQ RNQGGAQDMA QDPFGFGGLD
DIFRAMQGGN PEFNNPQSSI PPTQPQGPTN NGGQNGRSGN GNSLLGQYGI NMTQLAKDGK
IDPVIGRDSE ISRVVEILNR RTKNNPVLIG EAGVGKTAVV EGLAQQIVSG DVPAKLQNKQ
VIRLDVVSLV QGTGIRGQFE QRMQQLIKEV QDNPDIILFI DEIHEIVGAG NAEGGMDAGN
VLKPALARGE FQLIGATTLK EYRDIEKDSA LARRLQPVTV NEPSPEESVK ILQGIQKRYE
DYHHVKYSDD AIKAAVELSD RYIQDRFLPD KAIDFLDEAG SRKNLTINVV DPATIDEKIK
SAENQKQDAL KNEDYEKAAY YRDQVSKLEQ KKSDGNVDPS SIPEVTESDM QKIVEEKTEI
PVGELQAQEQ QQLKNLGPNL EEHVIGQNDA VEKVARAIRR NRVGFNGTGR PIGSFLFVGP
TGVGKTELAK QLAYQLFGSK DSMIRFDMSE YMEPHSVAKL IGSPPGYVGY DEAGQLTEQV
RRHPYSLILL DEVEKAHPDV LHMFLQILDD GRLTDSQGRT VSFKDTIIIM TSNAGTGDSE
ANVGFAAAAS GKTHSVIDKL TNYFKPELLN RFDDVIEFNP LSKENLQQIV SLMIDDVNEM
LAQQNLNIEV SDAAKKKLVD LGYNPAMGAR PLRRVIQEEI EDKVADYYLD HSADAKLYAD
VKDDEIVISS SSDTQSTSED NQHSEDEDK
//