ID E1WXD1_HALMS Unreviewed; 784 AA.
AC E1WXD1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:CBW27448.1};
GN Name=clpA {ECO:0000313|EMBL:CBW27448.1};
GN OrderedLocusNames=BMS_2669 {ECO:0000313|EMBL:CBW27448.1};
OS Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS (Bacteriovorax marinus).
OC Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC Halobacteriovoraceae; Halobacteriovorax.
OX NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW27448.1, ECO:0000313|Proteomes:UP000008963};
RN [1] {ECO:0000313|Proteomes:UP000008963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC {ECO:0000313|Proteomes:UP000008963};
RX PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA Williams H.N., Stine O.C.;
RT "A small predatory core genome in the divergent marine Bacteriovorax
RT marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL ISME J. 7:148-160(2013).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FQ312005; CBW27448.1; -; Genomic_DNA.
DR RefSeq; WP_014245223.1; NC_016620.1.
DR AlphaFoldDB; E1WXD1; -.
DR STRING; 862908.BMS_2669; -.
DR KEGG; bmx:BMS_2669; -.
DR PATRIC; fig|862908.3.peg.2547; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_7; -.
DR OMA; HDKFLPD; -.
DR Proteomes; UP000008963; 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; 2.
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:CBW27448.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CBW27448.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008963};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..169
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 784 AA; 87394 MW; 6E430BCECF94EAD1 CRC64;
MMSKKLEEII NQAIQIANEK KHEYLTLETV LISMLDDDQV IEVLNDLGAD VDQIQTDLVE
FLNDKDNFSI LTDEQVQNLS EQQFVDEELR KLASENGIKY QPEISLSLQR VIQRAAIHVQ
SSGKRHIMGI NILVSMFQEK ESFALYSIQK HGIERFDVVR YIAHGADEPA NSDEEFISDS
ELEGGITPSR INKEKKENAA LNEFCVNLNS LAKKNKIDPL IGREDELERI VEILCRRRKN
NPLLVGEAGV GKTAIVEGLA KSIVEGNVPE VLEGTTIFSL DMAALLAGAK FRGDFEKRLK
NVLKDLDTIQ DKGEKAILFI DEIHTVMGAG ATNGGSMDAS NLLKPALSSG RVRCVGSTTH
DEFRKFIEKD HAFSRRFQKI DVDEPSLDDT YQILKGLKPK FEEHHGVKYS NAVLRAAVDL
SDKFLGDRKN PDKSIDVVDE VGARVHLLPK NKRKKNISKK DVEAIISKLA KIPEISVTGS
DKDRLKNLKS NLHLVIYGQD EAVEKVSDAI ILSRSGLGHE NKPMANFLFA GPTGVGKTEL
ARQLAHNLGS HLERFDMSEY MEKHSVAKLI GAPPGYVGYD NGGLLTDAVK KNPHCILLLD
EIEKAHPDIY NILLQVMDHG SLTDSQGRTT DFRNTVIIMT TNAGAKQMDA GSIGLGQAKF
EGNTAKRDQT LKNFFSPEFR NRLDGIIHFN KLGSEFIVKI VDKFLLDLET RLAAKNVEIE
VTQKAKLWLA DTGYDPKMGA RPIGRIIDQQ IKKPLSNEVL FGELAKGGKV IVDYDGEEIT
FKYE
//