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Database: UniProt
Entry: A0A2T0TYW3_9SPHI
LinkDB: A0A2T0TYW3_9SPHI
Original site: A0A2T0TYW3_9SPHI 
ID   A0A2T0TYW3_9SPHI        Unreviewed;       392 AA.
AC   A0A2T0TYW3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:PRY50861.1};
GN   ORFNames=B0I27_10868 {ECO:0000313|EMBL:PRY50861.1};
OS   Arcticibacter pallidicorallinus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Arcticibacter.
OX   NCBI_TaxID=1259464 {ECO:0000313|EMBL:PRY50861.1, ECO:0000313|Proteomes:UP000238034};
RN   [1] {ECO:0000313|EMBL:PRY50861.1, ECO:0000313|Proteomes:UP000238034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9313 {ECO:0000313|EMBL:PRY50861.1,
RC   ECO:0000313|Proteomes:UP000238034};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01250}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:PRY50861.1}.
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DR   EMBL; PVTH01000008; PRY50861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0TYW3; -.
DR   Proteomes; UP000238034; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   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; 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   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:0000313|EMBL:PRY50861.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:PRY50861.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:PRY50861.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238034};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..30
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
SQ   SEQUENCE   392 AA;  43738 MW;  9829A8E2B31220DE CRC64;
     MLIAGLDAHI CDKCVAQANQ ILAEELSVRK TKSTGSSLTL MKPLEIKKHL DQYVIGQDEA
     KKVLSVAVYN HYKRLNQKVE KDEIEIEKSN IIMVAETGTG KTLLAKTIAK ILHVPFCICD
     ATVLTEAGYV GEDVESILTR LLQAADYDVA SAERGIVYID EVDKIARKSD NPSITRDVSG
     EGVQQALLKI LEGTIVNVPP QGGRKHPDQK MIAVNTNNIL FICGGAFDGI DRKIANRLKT
     QTVGYRINDD DANIDLKNLY KYITPQDLRS FGLIPELIGR LPVVTHLNPL DRDALISILT
     EPKNSLVKQY QKLFEYEDIK LDFDKEVLEF IVDKAMEFKL GARGLRSICE AIMIDAMFEV
     PSQKGKNKEL FITLSYALEK FAKSDIKKLK VA
//
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