GenomeNet

Database: UniProt
Entry: A0A1I2ZPM3_9BACT
LinkDB: A0A1I2ZPM3_9BACT
Original site: A0A1I2ZPM3_9BACT 
ID   A0A1I2ZPM3_9BACT        Unreviewed;       865 AA.
AC   A0A1I2ZPM3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SFH39566.1};
GN   ORFNames=SAMN05421739_1173 {ECO:0000313|EMBL:SFH39566.1};
OS   Pontibacter chinhatensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1436961 {ECO:0000313|EMBL:SFH39566.1, ECO:0000313|Proteomes:UP000198724};
RN   [1] {ECO:0000313|EMBL:SFH39566.1, ECO:0000313|Proteomes:UP000198724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LP51 {ECO:0000313|EMBL:SFH39566.1,
RC   ECO:0000313|Proteomes:UP000198724};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOOT01000017; SFH39566.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2ZPM3; -.
DR   STRING; 1436961.SAMN05421739_1173; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000198724; 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:SF18; HEAT SHOCK PROTEIN 104; 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:SFH39566.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFH39566.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          442..477
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          148..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          832..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          438..488
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        164..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  96840 MW;  56A19FD19E7E8160 CRC64;
     MEAKFSNRVK EVISLSREEA IRLGHDYIGT EHLVLGMIRE GEGTAISLLK KLGVSIDELK
     YALEQATRNT ASQSSNITGS IPLTKQTEKV LKITYLEAKI FKSDIIGTEH LLLSILRDED
     NISSQILAKF NVNYEAIRDS LDYHSNNPLA SSDTDDSDDS DKLFGSSSSR SGSSSSKKPG
     EKSRTPVLDN FGRDLTKLAE DDKLDPIVGR EKEIERVAQV LSRRKKNNPI LIGEPGVGKT
     AIAEGLALRI IQKKVSRVLF NKRVVTLDLA SLVAGTKYRG QFEERMKAVM NELEKSPDVI
     LFIDELHTIV GAGGASGSLD ASNMFKPALA RGEIQCIGAT TLDEYRQYIE KDGALARRFQ
     IVMVDPTTPE ETMEILHNIK DKYQDHHHVN YTDKAIEACV KLSDRYMSDR FLPDKAIDIL
     DEAGARVHIN NIVVPDDILK LEEQIENIKV EKNRVVKSQK YEEAAQLRDK EKKLIDQLET
     AKRNWEDETK KKRYQVKEEN VAEVIAMMTG IPVKRIAQNE GQKLLNMGEE LKGKVIGQDK
     AITQLVKAIQ RTRVGLKDPK KPIGSFVFLG PTGVGKTELA KVLATYLFDK EDSLVRIDMS
     EYMEKFSVSR LVGAPPGYVG YEEGGQLTEK IRRKPYSVVL LDEIEKAHPD VYNLLLQVLD
     DGILTDGLGR KVDFRNTIII MTSNIGARDL QDFGAGIGFM SKAKQENVDD IMKGTIASAL
     KKTFSPEFLN RLDDVIVFNS LGREDMHKII ELSLGKLFKR VESLGYTIEL TKEAKDFVAE
     KGYDPKYGAR PLNRAIQKYI EDPIAEEILK AEINQGDVIL IDYKEGEEKL TFTSKKSNGK
     KAKQANDGEE ETEPTKSTDT DKTKE
//
DBGET integrated database retrieval system