ID A0A099EXM9_9RHOB Unreviewed; 964 AA.
AC A0A099EXM9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:KGJ03185.1};
GN ORFNames=IC63_13620 {ECO:0000313|EMBL:KGJ03185.1};
OS Paracoccus sphaerophysae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=690417 {ECO:0000313|EMBL:KGJ03185.1, ECO:0000313|Proteomes:UP000029917};
RN [1] {ECO:0000313|EMBL:KGJ03185.1, ECO:0000313|Proteomes:UP000029917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ03185.1,
RC ECO:0000313|Proteomes:UP000029917};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ03185.1, ECO:0000313|Proteomes:UP000029917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ03185.1,
RC ECO:0000313|Proteomes:UP000029917};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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:KGJ03185.1}.
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DR EMBL; JRKS01000055; KGJ03185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099EXM9; -.
DR STRING; 690417.IC63_13620; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000029917; 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; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF145; CLPA/B PROTEASE ATP BINDING SUBUNIT-RELATED; 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; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KGJ03185.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KGJ03185.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029917};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 115..255
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 917..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 524..574
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 964 AA; 106084 MW; 2E782324CA0B58B9 CRC64;
MANGACDICG RPATARVRAS VNGRVQNMEL CDQHYSEMAR RSGRSASPLE SLFGRRSLLD
EFFGESGFGS LFGDSPLRGG TPGPMGDGDD AVVDATFGEG APRRGSRRGG GRTIADRLSE
QGNKLLQDAA QKAGEFGRSE VDTEHLLLAL TASDVVKTIL EQFKVDVDDL RRQIENEAKR
GDAKTEGEIG VSPRLKDALN RAFIASNELG HSYVGPEHLL IGLAEEGEGL AAAMLRKLGL
TPQALRQQVT KVVGKGAEEG RVEAPSSTPD LDQFSRDLTK LAREGKLDPV IGRAREIETT
IEVLARRKKN NPVLIGEPGV GKTAIVEGLA QRIVAGEVPE ALRDKRLVEL NINSMVAGSK
YRGEFEERVQ KILKEITEEK DSLILFIDEM HTIVGAGQGG GEGGLDIANT FKPALARGEL
NLIGATTLNE YQKYIEKDAA LERRFQPVYV DEPTVAQTIM ILRGLRDTLE SHHKVTITDE
AIIAAAELSD RYITGRFMPD KAIDLIDQAA ARVKISATAR PVDVQELEAE VAQIKREQDY
AAARKQFDRA AELKKELEQK QKELDELLEI WKRDQASATA EVRADHVAQI VSKITGVPVT
ELTTEEKDKL LKLEEKLHER VIGQEEAIRA VADAVRLARA GLREGSGPTA TFLFLGPTGV
GKTELAKTLA EVIFGDQDAL IRIDMSEYGE RHAVARLVGA PPGYVGYDEG GQLTEKVRRR
PYSVVLLDEI EKAHPDVYNI LLQVFDDGRL TDGKGRVVDF TNTIIIATSN LGSDIIQRNL
TKRGSSEFDE AKQKSELMEV LRGHFRPEFI NRIDEIIVFH SLNQSEIRQI VELQLNRVKR
TALTQGVELE LDVSVVDHFA AVGFRPEFGA RELRRLIRSE LETELARELL SGRIEDGDKV
RVAWSADEQR VVFEKIVKDT SDDSQDDQAK AGIEEPSEVA EDKTDVPKPS VGDEVQSKDD
KSAE
//