ID B8CXC4_HALOH Unreviewed; 490 AA.
AC B8CXC4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Microtubule-severing ATPase {ECO:0000313|EMBL:ACL69943.1};
DE EC=3.6.4.3 {ECO:0000313|EMBL:ACL69943.1};
GN OrderedLocusNames=Hore_11930 {ECO:0000313|EMBL:ACL69943.1};
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL69943.1, ECO:0000313|Proteomes:UP000000719};
RN [1] {ECO:0000313|EMBL:ACL69943.1, ECO:0000313|Proteomes:UP000000719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
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DR EMBL; CP001098; ACL69943.1; -; Genomic_DNA.
DR RefSeq; WP_012636128.1; NC_011899.1.
DR AlphaFoldDB; B8CXC4; -.
DR STRING; 373903.Hore_11930; -.
DR KEGG; hor:Hore_11930; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_9; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000000719; Chromosome.
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:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACL69943.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000719};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..243
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 490 AA; 54509 MW; 7E3DA2AD17928C68 CRC64;
MVKEVGIGAG IGVLIILALK GFNILPVIFF GFLVFFLWQM LSPSLSISSQ TGIKEGNKKI
PHVKFDDIGG QETAKNELIE ALNFVKNLDR IKYMGIRPIK GILLSGPPGT GKTMLAKASA
RYTDSVFKAT SGSEFIEMYA GLGAKRVRQL FKEARQSAKK YGKSSAIVFI DEIDVVGGKR
GQVTSHLEYD QTLNQLLVEM DGLSVDDEVQ ILVMATTNRI DILDPALLRP GRFDRIVQVD
LPAKEGRLSI LKIHTSNKPL AEEVNLEQIA RETFGFSGAH LENLTNEAAI MAMRGNEDQI
HQKHFLEAID KVIMGEKLDR RPGKEELKRI AVHETGHALV GEKFCPGSVS AITITSRGKA
LGYVRHNPRD DMYLQTRDYI EKQIGISIAG AIAEDILLND RSTGATNDFK KAVKLANKMV
ASGMTDLGVV EESTVPKQLL HEERTKIFKK VEKKVRNIIN NNKEIMEKIT RKLVEEERFS
GDELRRLLNN
//
