ID A0A0Q1AHR7_9CORY Unreviewed; 871 AA.
AC A0A0Q1AHR7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC1 {ECO:0000313|EMBL:KQB86200.1};
GN Name=clpC1 {ECO:0000313|EMBL:KQB86200.1};
GN ORFNames=Clow_01554 {ECO:0000313|EMBL:KQB86200.1};
OS Corynebacterium lowii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB86200.1, ECO:0000313|Proteomes:UP000050488};
RN [1] {ECO:0000313|EMBL:KQB86200.1, ECO:0000313|Proteomes:UP000050488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130206 {ECO:0000313|EMBL:KQB86200.1,
RC ECO:0000313|Proteomes:UP000050488};
RA Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT "Corynebacteirum lowii and Corynebacterium oculi species nova, derived from
RT human clinical disease and and emended description of Corynebacterium
RT mastiditis.";
RL Submitted (OCT-2015) 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:KQB86200.1}.
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; LKEV01000004; KQB86200.1; -; Genomic_DNA.
DR RefSeq; WP_055178166.1; NZ_LKEV01000004.1.
DR AlphaFoldDB; A0A0Q1AHR7; -.
DR STRING; 1544413.Clow_01554; -.
DR PATRIC; fig|1544413.3.peg.1556; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000050488; 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:KQB86200.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:KQB86200.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KQB86200.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050488};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 445..480
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 145..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 96249 MW; 0708B48B4005257A CRC64;
MFERFTDRAR RVIVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SMGISLDDVR
REVEEIIGHG TQPHTGHIPF TPRAKKVLEL SLREGLQMGH KYIGTEFLLL GLIREGEGVA
AQVLVKLGAD LPRVRQQVIQ LLSGYEGGQG TNPENSQPSN SGPVGAGAAA GPGGGGGRGG
SSGDRSNSLV LDQFGRNLTQ AAKDGKLDPV VGREKEIERV MQVLSRRTKN NPVLIGEPGV
GKTAVVEGLA LDIVNGKVPE TLKDKQLYSL DLGSLVAGSR YRGDFEERLK KVLKEINQRG
DIILFIDEIH TLVGAGAAEG AIDAASLLKP KLARGELQTI GATTLDEYRK HIEKDAALER
RFQPVQVPEP SVELSVEILK GLRDRYEAHH RVSITDSALE AAARLSDRYI NDRYLPDKAV
DLIDEAGARM RIKRMTAPEG LREVDERIAA VRKENEAAID AQDFEKAAGL RDKERKLGEE
RSEKEKQWRD GDLDEIAEVG EEQIAEVLGN WTGIPVFKLT EEESSRLLNM EAELHKRIIG
QDDAVKSVSR AIRRTRAGLK DPKRPSGSFI FAGPSGVGKT ELSKALAEFL FGEEDALIQI
DMGEFHDRFT ASRLFGAPPG YVGYEEGGQL TEKVRRKPFS VVLFDEIEKA HKEIYNTLLQ
VLEEGRLTDG QGRVVDFKNT VLIFTSNLGT QDISKAVGMG FTGSSENDEA AQYQRMKNKV
HDELKKHFKP EFLNRIDDTV VFHQLTQDQI VEMVELLIGR VEKMLAAKDM GIELTEKAKA
LLAKRGFDPV LGARPLRRTI QRDIEDAMSE KILFGELGAG EIVTVDVEGW DGESKETQDA
KFTFTPRPKP LPEDAFAEVE EEVREVTQDA K
//
