ID A0A2U3MUF0_9GAMM Unreviewed; 758 AA.
AC A0A2U3MUF0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SPL69024.1};
GN Name=clpA {ECO:0000313|EMBL:SPL69024.1};
GN ORFNames=KPC_0202 {ECO:0000313|EMBL:SPL69024.1};
OS Acinetobacter stercoris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=2126983 {ECO:0000313|EMBL:SPL69024.1, ECO:0000313|Proteomes:UP000245974};
RN [1] {ECO:0000313|Proteomes:UP000245974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KPC-SM-21 {ECO:0000313|Proteomes:UP000245974};
RA Blom J.;
RL Submitted (MAR-2018) 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; OOGT01000005; SPL69024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3MUF0; -.
DR InParanoid; A0A2U3MUF0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000245974; 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:SPL69024.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SPL69024.1};
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"
SQ SEQUENCE 758 AA; 84117 MW; 6CA13DA4174B3DDB CRC64;
MLSRQLEVSL RLAVSMARQK RHEFLTVEHL LLALLDNDSA VNALKACGAD IVSLRKELEE
YVEQHTPKLG ENSDQAPHPT ESFDRILQRA IFHVQSSGGD RTVEGADVLV AMYSERDSFA
VYLLKRHQIN RLTLTQYLSH GTRKDEIQVE EENEDLEGEA NASQNAGPLE LYTVNLNIEA
QKGKTDPLIG REKEIERTAQ ILCRRRKNNP LLVGDPGVGK TSIAEGLAWL IVNGKAPKPL
ANAEVYSLDI GSLVAGTKYR GDFEKRLKQL LNALKKNPNA ILFIDEIHMI IGAGSSMGST
MDASNLIKPA LANGTLRCIG STTFQEYRQV FEKDHALSRR FQKIDVNEPS ISESIDILRG
LKSKFEDFHH VEYEDKALVS AVELSAKFIN DRFLPDKAID VIDEAGAQRR LKAENDGTLI
TVENIEDIVS KIARIPPKTV SKDDKSVLEH LERDLKRVVF GQDEAITALA SAIKLSRAGL
KSPDKPVGSF VFAGPTGVGK TEVTKQLAKL LGVELVRFDM SEYMERHAVS RLIGAPPGYV
GYDQGGLLTD AIHKNPHCVL LLDEIEKAHP DVFNLLLQVM DHGSLTDNNG RKSDFRNVII
VLTTNIGAES ISRTSIGFTE QDNSNDNQEA MKRAFSPEFR NRLDGVIQFK ALPTSVIESV
VDKFLTELQA QLDEKKVVLE VDQSARDWMA ENGYDRLMGA RPMQRLIQEH LKKPLAEMIL
FGELADHGGN VAVSVKKENG KAVGLKLEVF EDQTAEPA
//