ID A0A2T7FU28_9RHOB Unreviewed; 972 AA.
AC A0A2T7FU28;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:PVA05663.1};
GN ORFNames=DC363_14415 {ECO:0000313|EMBL:PVA05663.1};
OS Thalassorhabdomicrobium marinisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassorhabdomicrobium.
OX NCBI_TaxID=2170577 {ECO:0000313|EMBL:PVA05663.1, ECO:0000313|Proteomes:UP000244817};
RN [1] {ECO:0000313|EMBL:PVA05663.1, ECO:0000313|Proteomes:UP000244817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH-SD16 {ECO:0000313|EMBL:PVA05663.1,
RC ECO:0000313|Proteomes:UP000244817};
RA Ji X.;
RT "Pelagivirga bohaiensis gen. nov., sp. nov., a bacterium isolated from the
RT Bohai Sea.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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:PVA05663.1}.
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DR EMBL; QCYG01000009; PVA05663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7FU28; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000244817; 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; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF145; CLPA/B PROTEASE ATP BINDING SUBUNIT-RELATED; 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; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:PVA05663.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:PVA05663.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244817};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 104..244
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 71..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 513..563
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 73..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 106581 MW; BFA807206495C07B CRC64;
MANGICDICK RRPASFRAQV SVNGERQLME LCDEDYRKLA RQQRRSSSPL ESLFGGGSLF
DEFFGDSPFG NMSRRLSDDS DGTGGQRIPV SSGSRRGSGG AGIADRLSEQ GNKLLQEAAQ
KAGELGRSEV DTEHLLFALS HSDVVKTLLE QFKIDIDDLR RQIESEAPRG EGKEGGEIGV
SPRLKDALNR AFIASNELGH SYVGPEHLLI GLAEEGEGLA ADILRKYGLT PQALRQQVTK
VVGRGAEEGR VDAPSNTPDL DEFSRDLTKL AREGKLDPVI GRAREIETTI EVLARRKKNN
PVLIGEPGVG KTAIIEGLAQ RIVAGEVPEA LRDKRLVELN INSMVAGSKY RGEFEERIQK
VLKEIEANKD DLVLFIDELH TIMGAGQGGG EGGLDVANTF KPALARGELN LIGATTLNEY
QKHIEKDAAL ERRFQPVYVD EPSVAQTIMI LRGLRDMLES HHKVTITDEA IVASAELADR
YISGRFMPDK AIDLIDQAAA RVKISATARP VDVQELEAEV AQIKREQDYA AARKQFDRAA
DLKHELEEKQ TELDALLETW KRDRASARAE VRTDHIAQIV SKLTGIPVTD LTSEERENLL
KLEERLHERV IGQNEAIDAV ADAVRLARAG LRDGPAPTAT FLFLGPTGVG KTELAKALAE
VVYGDEDAMI RIDMSEYGER HTVARLVGAP PGYVGYDEGG QLTERVRRRP YSVVLLDEIE
KAHGDVYNIL LQVFDDGRLT DGKGRVVDFT HTIIIATSNL GSDIIQRNLK KRGTKQFDET
KQHAELMEVL RSHFRPEFLN RIDEIIVFHS LNQSEIRKIV GLQLARVART ALNQGVELDF
DESVTDHFAA VGFQPEFGAR ELRRLIRSEL ETELARAMLS GSVEDGDRVR VAWSAEEQKI
TFEKLEATDV TDAPAADVAE DAAPAKPDGG DRDGAAETPE HSADAAAADD KAKPGKPATA
DETDKGGADA TT
//