ID E4PRD5_MARAH Unreviewed; 756 AA.
AC E4PRD5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:ADP97844.1};
GN Name=clpA {ECO:0000313|EMBL:ADP97844.1};
GN OrderedLocusNames=HP15_2080 {ECO:0000313|EMBL:ADP97844.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP97844.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP97844.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP001978; ADP97844.1; -; Genomic_DNA.
DR RefSeq; WP_014577423.1; NC_017506.1.
DR AlphaFoldDB; E4PRD5; -.
DR STRING; 225937.HP15_2080; -.
DR KEGG; mad:HP15_2080; -.
DR PATRIC; fig|225937.3.peg.2095; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_6; -.
DR Proteomes; UP000007077; Chromosome.
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:0043335; P:protein unfolding; IEA:InterPro.
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; IPR004176; Clp_R_dom.
DR InterPro; IPR013461; ClpA.
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 NCBIfam; TIGR02639; ClpA; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 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.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 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 Hydrolase {ECO:0000313|EMBL:ADP97844.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ADP97844.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 145..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 83933 MW; CAB1C6C0BBA9F4E0 CRC64;
MLSKDLEITL NTAFKNARDK RHEFMTVEHL LLALLDNESA VGVLKACGAD LKRLQEELVE
FVDSTTPLIP SSDSERETQP TLGFQRVLQR AVFHVQSSGK KEVTGANVLV AIFSEQESQA
VYVLKKQSIA RIDVVNFVSH GISRVQGAED QESQDQASHE EAGEEGGQSK PLESYATNLN
EQARQGRIDP LIGREHEVER VVQILVRRRK NNPLLVGEAG VGKTAIAEGL AKRIVDGQVP
DIISDAVVYS LDLGALLAGT KYRGDFEKRL KGLLAELKKE NHAILFIDEI HTIIGAGSAS
GGVMDASNLL KPMLSSGEIR CIGSTTFQEF RGIFEKDSAL ARRFQKIDVN EPSVEDTYQI
LKGLKPNFEK HHDLKYTDKA LRVAAELSDR YITDRHLPDK AIDVIDEAGA RQRLQPEGKR
KKTVDVTEIE DVVANIARIP PKNVSTSDKD LLRNLERDLK MTVFGQDPAI ESLSTAIKLA
RAGLKAPEKP EGAFLFAGPT GVGKTEVTKQ LAKVLGIELV RFDMSEYMER HTVSRLIGAP
PGYVGYDQGG LLTESVNKHP HCVLLLDEIE KAHPEVFNLL LQVMDHGTLT DNNGRKADFR
HVILVMTTNA GAESMARRSI GFSEQDHSTD GMEIISKTFT PEFRNRLDGI IQFGDLQIDT
ITHVVDKFLT ELQAQLDEKH VVLHVDDEAK AWLAEKGYDV TMGARPMSRL IQDKIKRPLA
EQILFGRLSE KGGDVFIHLR DDELVFEYED EPAEAV
//
