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Database: UniProt
Entry: A0A151JUY3_9HYME
LinkDB: A0A151JUY3_9HYME
Original site: A0A151JUY3_9HYME 
ID   A0A151JUY3_9HYME        Unreviewed;       696 AA.
AC   A0A151JUY3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial {ECO:0000313|EMBL:KYN37348.1};
GN   ORFNames=ALC56_08251 {ECO:0000313|EMBL:KYN37348.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN37348.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN37348.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN37348.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN37348.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ981713; KYN37348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151JUY3; -.
DR   STRING; 34720.A0A151JUY3; -.
DR   Proteomes; UP000078541; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KYN37348.1};
KW   Hydrolase {ECO:0000313|EMBL:KYN37348.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:KYN37348.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        83..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          174..227
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          150..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   696 AA;  77176 MW;  11BD345ADA3EEBBA CRC64;
     MRTTLYSMPL SVGSIYNLRY QYYSCLYWFQ SPAILSSSLV LQLEQTGREA YNLMQVNVIG
     LLHESPHHEY VEKMPVILRY PRMVVNLYAT ISVLSPSSTF VLFAINNIMF RQFGHRIGVT
     PSFLILVIIK RVHKIVRVVV ASRGLTISGS LSKAPTEPTP PSKDTISSSG SSSSGTGGGK
     KSTLTCPKCG DPCTHVETFV SSTRFVKCEK CHHFFVVLSE IDSKRSLKEA LRPEDSKQGF
     YRKPPPPPKK IFEYLNRHVV GQEYAKKVLS VAVYNHYKRI YNNLPTQNSQ AQTNVNPVST
     QETNHPFTHR DLLHISGLGN PFPGIGFQHT VNPGSEQKAS SQSAPGSAIL DSKQHQLKLE
     KSNILLLGPT GSGKTLLAQT IAQCLDVPFA ICDCTTLTQA GYVGEDIESV IAKLLQDANY
     VVDRAQMGIV FLDEVDKIGA IPGIHQLRDV GGEGVQQGML KMLEGTIVNV PERNSSRKLR
     GEMLQVDTTN ILFVASGAYS GLDRLIARRK SEKYLGFGAT PAVESPGRRA ATLADVANMS
     PSTERDNKEK DMLLQQVEAR DLIDFGMIPE FVGRFPVLVP FHTLDRDMLA RILTEPKNAI
     IPQYQMLFSM DKVELTFDIH ALNAIASLAM ERKTGARGLR AIMESLLLEP MFEVPGSDIM
     SVHITEQCVK GVEKPQYVKR DDSNDDDIQQ AQHVHN
//
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