ID A0A502GDJ1_9PROT Unreviewed; 788 AA.
AC A0A502GDJ1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:TPG59106.1};
GN Name=clpA {ECO:0000313|EMBL:TPG59106.1};
GN ORFNames=EAH89_07070 {ECO:0000313|EMBL:TPG59106.1};
OS Roseomonas nepalensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Roseomonas.
OX NCBI_TaxID=1854500 {ECO:0000313|EMBL:TPG59106.1, ECO:0000313|Proteomes:UP000317078};
RN [1] {ECO:0000313|EMBL:TPG59106.1, ECO:0000313|Proteomes:UP000317078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S9.3B {ECO:0000313|EMBL:TPG59106.1,
RC ECO:0000313|Proteomes:UP000317078};
RX PubMed=31206918;
RA Altshuler I., Hamel J., Turney S., Magnuson E., Levesque R., Greer C.,
RA Whyte L.G.;
RT "Species interactions and distinct microbial communities in high Arctic
RT permafrost affected cryosols are associated with the CH4 and CO2 gas
RT fluxes.";
RL Environ. Microbiol. 0:0-0(2019).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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:TPG59106.1}.
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DR EMBL; RCZP01000004; TPG59106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A502GDJ1; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000317078; 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: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:TPG59106.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TPG59106.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000317078};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 143..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 86294 MW; 675D0CFC9D1049EA CRC64;
MLSRNLEQTL HRALGLASER RHEYATLEHL LLSLAEDSDA TTVLRACGVD VDKLKRDLAE
FLDKDLAGLV TDRGGDPKPT AGFQRVVQRA AIHVQSSGRD EVTGANVLVA LFSERESHAV
YFLQLQDMTR LDAVNFISHG IAKAPGRSTT RPVQGNAGKD GDEGGESRGG EERREGGAKR
GGDALSNYCV NLNKKAGQGK IDPLIGRADE IERTIQILCR RTKNNPLYVG DPGVGKTAIA
EGLAKRIIEE DVPEVLLKST IYALDMGSLL AGTRYRGDFE ERLKAVVNEL EQQPGAILFI
DEIHTVIGAG ATSGGAMDAS NLLKPALAQG TLRCIGSTTY KEYRQHFEKD RALVRRFQKI
DVNEPNVEDA VKILTGLKTN YEKHHKVKYT PEAIRGAVEL SVKYIHDRKL PDKAIDVIDE
VGASRMLLPE NKRRKTVTLK DVEDIVAKIA RIPPKSVSTD DKEVLKNLER DLRSMVFGQD
KAIETLSAAI KLSRAGLRDA EKPIGNYLFS GPTGVGKTEV AKQLSKTLGI ELIRFDMSEY
MERHSISRLI GAPPGYVGFD QGGLLTDSID QHPHAVLLLD EIEKAHQDLY NILLQVMDHG
KLTDHNGKTV DFRNVILIMT TNAGAADMAK PAIGFGSSVR VGEDEEAIKR MFTPEFRNRL
DAVVPFAGLT QEIVGNVVEK FVMQLEAQLA DRNVTIELSS SAKEWLAERG YDPLYGARPL
ARVIQEYVKK PLAEELLFGK LVKGGAVKVG FKDGALTFDI AEAPPPALPK PDEGSGDGES
EREPEAAN
//
