ID A0A6I2GAL5_9LACT Unreviewed; 414 AA.
AC A0A6I2GAL5;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175,
GN ECO:0000313|EMBL:MRI84810.1};
GN ORFNames=GF867_03130 {ECO:0000313|EMBL:MRJ46562.1}, GIY09_02710
GN {ECO:0000313|EMBL:MRI84810.1}, GIY11_00830
GN {ECO:0000313|EMBL:MRI80576.1};
OS Fundicoccus ignavus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Fundicoccus.
OX NCBI_TaxID=2664442 {ECO:0000313|EMBL:MRI84810.1, ECO:0000313|Proteomes:UP000430975};
RN [1] {ECO:0000313|EMBL:MRJ46562.1, ECO:0000313|Proteomes:UP000440066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 109652 {ECO:0000313|EMBL:MRJ46562.1,
RC ECO:0000313|Proteomes:UP000440066};
RA Siebert A., Huptas C., Wenning M., Scherer S., Doll E.V.;
RT "Characterisation of Fundicoccus ignavus gen. nov. sp. nov., a novel genus
RT of the family Aerococcaceae from bulk tank milk.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000430975, ECO:0000313|Proteomes:UP000469870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 109653 {ECO:0000313|EMBL:MRI80576.1,
RC ECO:0000313|Proteomes:UP000469870}, and WS4759
RC {ECO:0000313|EMBL:MRI84810.1, ECO:0000313|Proteomes:UP000430975};
RA Siebert A., Huptas C., Wenning M., Scherer S., Doll E.V.;
RT "Characterisation of Fundicoccus ignavus gen. nov. sp. nov., a novel genus
RT of the family Aerococcaceae isolated from bulk tank milk.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It
CC directs the protease to specific substrates. Can perform chaperone
CC functions in the absence of ClpP. {ECO:0000256|HAMAP-Rule:MF_00175}.
CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC into a disk-like structure with a central cavity, resembling the
CC structure of eukaryotic proteasomes. {ECO:0000256|HAMAP-Rule:MF_00175}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|HAMAP-
CC Rule:MF_00175, ECO:0000256|PROSITE-ProRule:PRU01250}.
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:MRI84810.1}.
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DR EMBL; WJQR01000001; MRI80576.1; -; Genomic_DNA.
DR EMBL; WJQS01000002; MRI84810.1; -; Genomic_DNA.
DR EMBL; WJQT01000002; MRJ46562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6I2GAL5; -.
DR Proteomes; UP000430975; Unassembled WGS sequence.
DR Proteomes; UP000440066; Unassembled WGS sequence.
DR Proteomes; UP000469870; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19497; RecA-like_ClpX; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 6.20.220.10; ClpX chaperone, C4-type zinc finger domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00175; ClpX; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR046425; ClpX_bact.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
DR InterPro; IPR038366; Znf_CppX_C4_sf.
DR NCBIfam; TIGR00382; clpX; 1.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR Pfam; PF06689; zf-C4_ClpX; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SMART; SM00994; zf-C4_ClpX; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00175};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW Hydrolase {ECO:0000313|EMBL:MRI84810.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00175}; Protease {ECO:0000313|EMBL:MRI84810.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000430975};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT DOMAIN 1..54
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 118..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 414 AA; 46128 MW; 2002ECE3F24B1CE8 CRC64;
MAKKTPRAND YFCSFCGKSQ DEVNKIIAGP DVFICDECVE LCKSIIDEEM KHEKQSAPIQ
VLKPSEIMAT LDQYVIGQKE AKKALSVAVY NHYKRVNHEG AFEDDIELHK SNICLIGPTG
SGKTYLAQSL ARILNVPFAI ADATTLTEAG YVGEDVENIL LKLVQAADYD LERAEKGIIY
IDEIDKISRK SENTSITRDV SGEGVQQALL KILEGTEANI PPKGGRKHPN QEFLKLDTSQ
ILFIVGGAFA GIENIVKERL GSKVIGFGSV NTKLDSSKSY MQQVTPEDLL KFGLIPEFIG
RLPVMASLEE LTEADLINIL TQPKNALVKQ YQRLLELEDV ELEFEDGALE EIAKRAIERE
TGARGLRSII EAVMLDVMFE VPNRDDIKKI VITRENVIGD SEPNYYNEEN RKIS
//
