ID A0A097EJC8_9SPHN Unreviewed; 771 AA.
AC A0A097EJC8;
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 ClpX {ECO:0000313|EMBL:AIT07671.1};
GN Name=clpA {ECO:0000313|EMBL:AIT07671.1};
GN ORFNames=MC45_16290 {ECO:0000313|EMBL:AIT07671.1};
OS Sphingomonas taxi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT07671.1, ECO:0000313|Proteomes:UP000033200};
RN [1] {ECO:0000313|EMBL:AIT07671.1, ECO:0000313|Proteomes:UP000033200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT07671.1,
RC ECO:0000313|Proteomes:UP000033200};
RA Zhou Y., Ma T., Liu T.;
RT "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT RASTools.";
RL Submitted (SEP-2014) 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; CP009571; AIT07671.1; -; Genomic_DNA.
DR RefSeq; WP_038665433.1; NZ_CP009571.1.
DR AlphaFoldDB; A0A097EJC8; -.
DR STRING; 1549858.MC45_16290; -.
DR KEGG; stax:MC45_16290; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_5; -.
DR Proteomes; UP000033200; 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:AIT07671.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AIT07671.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 145..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 84380 MW; 7FF99A5827514DAC CRC64;
MPSFAPALET TLHKALEAAS SRRHEYATLE HLLLALIGDE HASKVMEACH VELGDLKTTV
AHYLDTELDA LKVDAATDPS PTSGFQRVVQ RAILHVQSSG RDEVTGANVL VALFSERESY
AVYFLQQQDM SRLDAVSFIS HGVGKGGAAT EATTPKGAED DKPAKGQEKG KTESALKQFT
VDLNEKAKIG KVDPLIGRGP EVDRTIQILC RRSKNNPLYV GDPGVGKTAI AEGLARKIVE
GEVPDVLLEA VIYSLDMGAL LAGTRYRGDF EERLKAVVNE LEKLPHAVLF IDEIHTVIGA
GATSGGAMDA SNLLKPALSG GTIRCIGSTT YKEFRNHFEK DRALLRRFQK IDVNEPTIED
TIKILAGLRS AFEDHHNVKY TPDAIKSAVE LSARYINDRK LPDKAIDVID EVGAMQMLVP
LNKRKKTITA KEIEQVIATM ARIPPKSVST DDKAALESLE TDLKRVVFGQ NSAIEKLASA
IKLARAGLRE PEKPIGNYLF TGPTGVGKTE VAKQLSSILG IPLQRFDMSE YMERHSVSRL
IGAPPGYVGF DQGGLLTDAV DQNPHCVLLL DEIEKAHPDL FNILLQVMDN GRLTDQHGKS
VDFRNVILIM TTNAGASDMA RETVGFGNLT REGEDEQAVQ KMFTPEFRNR LDAIVPFGYL
PTEVVARVVD KFILQLELQL ADRNVHINLD DAAKSWLTEK GYDKLYGARP MGRLIQEKIK
QPLAEELLFG KLVHGGEVTV RMKDGALSFG IEPAAPKKPK KKGKAEPVDA K
//
