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Database: UniProt
Entry: A0A2H9VS45_9SPHI
LinkDB: A0A2H9VS45_9SPHI
Original site: A0A2H9VS45_9SPHI 
ID   A0A2H9VS45_9SPHI        Unreviewed;       844 AA.
AC   A0A2H9VS45;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:PJJ83646.1};
GN   ORFNames=CLV57_0634 {ECO:0000313|EMBL:PJJ83646.1};
OS   Mucilaginibacter auburnensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1457233 {ECO:0000313|EMBL:PJJ83646.1, ECO:0000313|Proteomes:UP000242687};
RN   [1] {ECO:0000313|EMBL:PJJ83646.1, ECO:0000313|Proteomes:UP000242687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28175 {ECO:0000313|EMBL:PJJ83646.1,
RC   ECO:0000313|Proteomes:UP000242687};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:PJJ83646.1}.
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DR   EMBL; PGFJ01000001; PJJ83646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H9VS45; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000242687; 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: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; 1.10.1780.10; Clp, N-terminal domain; 1.
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; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
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   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; PF02861; Clp_N; 2.
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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:PJJ83646.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:PJJ83646.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:PJJ83646.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242687};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          438..473
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          146..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  94259 MW;  8982164ECCA66BF2 CRC64;
     MEAKFSPRVK DVIQYSREEA LRLGHDYIGT EHLLLGLIRD GDGVAIKLLK ELAVDTARLR
     RSVEDAVKGT IGTNVHIGSI PLTKQAEKVL KITYLEAKIF KSDVIGTEHL LLSILRDEDN
     IASQILMQFN VNYEIFKGEV EAHKNNITDE MPGSPTGGDD DFKEEEAFNQ PKKVSDIKSK
     TPVLDNFGRD LTRAAEDGKL DPIVGREQEI ERVSQILSRR KKNNPILIGE PGVGKSAIAE
     GLALRIVQRK VSRVLFNKRV VTLDLASLVA GTKYRGQFEE RMKAVMNELE KSPDVILFID
     EIHTIVGAGG ASGSLDASNM FKPALARGEI QCIGATTLDE YRQYIEKDGA LDRRFQKVMI
     EPASISETIE ILNRIKEKYE EHHGVTYTQE AIEACVNLTT RYITDRFLPD KAIDALDEAG
     SRVHLTNIHV PQEILDIENK IEQIKLEKNK VVRSQKYEEA AKLRDTEKHL LEELEQAKGV
     WEAETKSKRY TVTEDNVAEV VAMMTGIPVQ KVGQADSQKL LNMSEKIGKK IIGQDDAVKK
     LARAIQRTRA GLKDPKKPIG SFIFLGPTGV GKTELAKELA RFMFDTEDAL IQIDMSEYME
     KFAVSRLVGA PPGYVGYEEG GQLTEKVRRK PYAVVLLDEI EKAHPDVFNI LLQVLDEGQL
     TDSLGRKVDF RNAIIIMTSN IGARQLKDFG QGVGFSTNAQ TTQADAHSRG VIENALKRAF
     APEFLNRIDD VIVFNSLGKE EIFKIIDIEL ASLFGRVHAL GYQIELTEAA KDFIADKGYD
     SQFGARPLKR AIQKYLEDPI AEEILKGELG EAELMVVDYD KDTNEIKVSA KKASGKEPKQ
     EEQD
//
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