ID A0A101D553_9GAMM Unreviewed; 758 AA.
AC A0A101D553;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:KUJ89167.1};
GN Name=clpA {ECO:0000313|EMBL:KUJ89167.1};
GN ORFNames=XD36_0382 {ECO:0000313|EMBL:KUJ89167.1};
OS Halomonas sp. 54_146.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1635257 {ECO:0000313|EMBL:KUJ89167.1, ECO:0000313|Proteomes:UP000053192};
RN [1] {ECO:0000313|Proteomes:UP000053192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUJ89167.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGEN01000003; KUJ89167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101D553; -.
DR STRING; 1635257.XD36_0382; -.
DR PATRIC; fig|1635257.4.peg.1764; -.
DR Proteomes; UP000053192; 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:KUJ89167.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KUJ89167.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 143..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 83350 MW; D531109380071815 CRC64;
MLSKELEMTL NTAFTVARSK RHEFMTVEHL LLALLDNASA ADVLKACGAN LDKLRSDLQD
FINSTTPLIP EGHGDRETQP TLGFQRVLQR AVFHVQSSGK SEVTGANVLV AIFSEQESQA
VYFLKQQSVA RVDAVNYIAH GISKVAGHGP SPSPSSSDSE EAEEGSNEGA AHPLTGYATN
LNEQARLGKI DPLIGRDHEL ERVVQILARR RKNNPLLVGE AGVGKTAIAE GLAKRIVEED
VPDVIADAVV YSLDMGALLA GTKYRGDFEK RLKSLLTELR KQPNAVLFID EIHTVIGAGA
ASGGVMDASN LLKPLLSSGE LRCIGSTTFQ EFRGIFEKDR ALARRFQKVD VMAPSVDDTI
KILKGLRSRF EEHHELKYTD GALESAARLA DRYINDRYLP DKAIDVIDEA GAHQRLLPPE
VRAKTIDVEQ VEAVVASIAR IPPKSVSSSD RKLLEKLDRD LKMLVFGQDE AIDSLSAAIK
LSRAGLKSPD KPVGSFLFAG PTGVGKTEVA KQLAHIMGIE LVRFDMSEYM ERHTVSRLIG
APPGYVGYDQ GGLLTEAVTK QPHCVLLLDE IEKAHPEVFN LLLQVMDHGR LTDNNGREAD
FRHVILIMTS NAGAEQSSRR SMGFQHQDHS TDAMEVIRRT FSPEFRNRLD GIIQFHALPV
SVVRNVVDKF LIELQAQLDE KRVQMDVDDM ARDWLADKGY DPDMGARPMA RLIQEKLKKP
LAEMILFGEL ADNGGIVHVS LEDGELHLST EAEMADAP
//