ID A0A434AYV1_9BACT Unreviewed; 833 AA.
AC A0A434AYV1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:RUT79802.1};
GN ORFNames=DLK05_00135 {ECO:0000313|EMBL:RUT79802.1};
OS Ancylomarina longa.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Ancylomarina.
OX NCBI_TaxID=2487017 {ECO:0000313|EMBL:RUT79802.1, ECO:0000313|Proteomes:UP000282985};
RN [1] {ECO:0000313|EMBL:RUT79802.1, ECO:0000313|Proteomes:UP000282985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T3-2 S1-C {ECO:0000313|EMBL:RUT79802.1,
RC ECO:0000313|Proteomes:UP000282985};
RA Fu T.;
RT "Parancylomarina longa gen. nov., sp. nov., isolated from sediments of
RT southern Okinawa.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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:RUT79802.1}.
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DR EMBL; RJJX01000001; RUT79802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A434AYV1; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000282985; 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; IPR028299; ClpA/B_CS2.
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; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:RUT79802.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RUT79802.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000282985};
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 435..470
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 146..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 431..488
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 833 AA; 92952 MW; D7D90DCB8E2E370B CRC64;
MDSKFSPRIK DVLSYSKEEA ERLGNTAIGT EHLFLGILRE GEGIAVDILI SLGVDLYDIR
KSIEKQLKSD SISELDQENI PLQRSAERVL KLIYLEAKAL KNNTIDTSHL LLAILKDEKS
MVTQILDDQS IDYNKVKQNL KTLFPKAQAD YPSDEPGGKS GMSGGDPKRS GVRGKSETPV
LDNFGIDITK SAEEGTLDPI VGRETEIERL AQILSRRKKN NPILIGEPGV GKSAIAEGLA
LRIIQKKVSR VLFGKRVVTL DLASIVAGTK YRGQFEERMK AILNELSKTS DIILFIDEIH
TIVGAGGATG SLDAANMLKP ALARGEIQCI GATTLDEYRQ NIEKDGALER RFQKVMVEPT
SPEETIVILN NIKERYEDHH SVYYTDEAIE ACVKLTSRYI SDRYLPDKAI DALDEAGSRV
HISNIHVPVI IEELEKKIEE TRQNKIKAVK AQKFELAASF RDKEKNFTDD LEREKDKWEQ
ELNLKKEKVS GEDIAEVVAM MTGVPVKRIA QAEGSRLLQM NTELQGRVVG QKDAIAKIVK
AIQRNRAGLK DPNKPIGTFI FLGPTGVGKT QLAKVLSEYL FDSHDALIRI DMSEYMEKFA
VSRLVGAPPG YVGYEEGGQL TEKVRRKPYS VVLLDEIEKA HPDVFNILLQ LLDDGQLTDS
LGRRVDFKNC IIIMTSNIGS RELKDFGKGI GFQAGSSESN DYTSSIIQKA LKKAFAPEFL
NRIDDLVMFN SLTQKDIHKI IDIELDGLYK RVNDLGYKIK ISSAAKDFIA EKGYDVQFGA
RPLKRAIQKY LEDEMAEVII KASISEGDTI SVGLDKSKMK ITTKILKHHK ELE
//
