ID A0A1I0QH10_9BACT Unreviewed; 815 AA.
AC A0A1I0QH10;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SEW26412.1};
GN ORFNames=SAMN05428988_3756 {ECO:0000313|EMBL:SEW26412.1};
OS Chitinophaga sp. YR573.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1881040 {ECO:0000313|EMBL:SEW26412.1, ECO:0000313|Proteomes:UP000198758};
RN [1] {ECO:0000313|EMBL:SEW26412.1, ECO:0000313|Proteomes:UP000198758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR573 {ECO:0000313|EMBL:SEW26412.1,
RC ECO:0000313|Proteomes:UP000198758};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOJF01000001; SEW26412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0QH10; -.
DR STRING; 1881040.SAMN05428988_3756; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198758; 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 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; IPR001270; ClpA/B.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
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; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:SEW26412.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:SEW26412.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SEW26412.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 199..342
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 550..693
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 718..808
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 815 AA; 90818 MW; B611B805FCC33466 CRC64;
MTLATYTIYA PEVQATIRIA QALAKEHHHV HYTPAHLLLA CLHREINLSA SLQAMDIDIY
YLEEWAEVRL DSLPKATRPS DEPEPDEHAA NVLQEADAVR LEYDLDAADA WCVLIALSTP
GVGFSYEQLK TFPLQREQLL THFSKTAAQP AAKSNGTGKT TALRYIYRLT DPQRLQSEHA
LAGRDAEVRT MIEILTRKGR SSILLIGEGG IGKTSMATAL ARAIINKQAP SQLHNTDVYT
LDYGTFIAGA AYKNELEDRL QQIIQQLQTA GRHILFIDNL HTLLDKQPNT AGGIANVLKA
ALGKGDITVV GTSTPEGFRK LIEPDSLLRH CFETITLSEP DEALAARMIQ AVVPDYESYY
GLTADHEVIA DAIRLARRYL KERSLPDSAI NLMDRTLAAV RTTQDTGEQI LADLKTKLEV
AGDSRPELLW WYQQLRQRLS ALLITRLQID QEISKIEDTG TLKAILLNLI EQLEPIVQNK
ATAVTTTDLA TMIAESTGIP LGKIQSGERE RLVNMDKELQ KRVVGQDHAL KTVAEAILES
RSGLSRPGQP IGSFFFLGPT GTGKTELAKS LADFLFQDER SMIRFDMSEF KEEHSAALLY
GAPPGYVGYE EGGLLVNKIR QQPYAVVLFD EIEKAHPSVF DIFLQIMDEG KLHDRLGKTG
DFSNALILFT SNIGSDVITQ SFRQGVIPPS QQLMELMTRH FRPEFLGRLT EIVPFGPIQQ
ENVVKIFDIH LQHLLQLLKQ QQISLEVSLA ARQQLAAEGY SPLYGARPLK EVIRSRLRKP
LSRMIIEGSL QPHTAVKLDI DKNGELQWDI VASEL
//