ID A0A2U9NSG4_9STRA Unreviewed; 672 AA. AC A0A2U9NSG4; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 02-DEC-2020, entry version 10. DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458}; DE EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458}; GN Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458, GN ECO:0000313|EMBL:AWT40073.1}; OS Biddulphia biddulphiana. OG Plastid; Chloroplast {ECO:0000313|EMBL:AWT40073.1}. OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae; OC Biddulphiophycidae; Biddulphiales; Biddulphiaceae; Biddulphia. OX NCBI_TaxID=1158022 {ECO:0000313|EMBL:AWT40073.1}; RN [1] {ECO:0000313|EMBL:AWT40073.1} RP NUCLEOTIDE SEQUENCE. RA Yu M., Ashworth M.P., Hajrah N.H., Khiyami M.A., Sabir M.J., Alhebshi A.M., RA Al-Malki A.L., Sabir J.S.M., Theriot E.C., Jansen R.K.; RT "Evolution of the Plastid Genomes in Diatoms."; RL Adv. Bot. Res. 85:129-155(2018). CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase. CC {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01458}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01458}; Stromal side {ECO:0000256|HAMAP- CC Rule:MF_01458}. 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, ECO:0000256|HAMAP- CC Rule:MF_01458}. CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase CC family. {ECO:0000256|ARBA:ARBA00010550}. CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family. CC {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}. 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; MG755805; AWT40073.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.58.760; -; 1. DR HAMAP; MF_01458; FtsH; 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; IPR005936; FtsH. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000642; Peptidase_M41. DR InterPro; IPR037219; Peptidase_M41-like. 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; SSF140990; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 1. DR PROSITE; PS00674; AAA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; Chloroplast {ECO:0000313|EMBL:AWT40073.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01458}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP- KW Rule:MF_01458}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; Plastid {ECO:0000313|EMBL:AWT40073.1}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01458}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01458}. FT TRANSMEM 6..26 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT TRANSMEM 156..178 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 245..384 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" FT NP_BIND 253..260 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT COILED 329..349 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 475 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 672 AA; 74662 MW; 26F5BC0CA4E33D8B CRC64; MLGNLFIITM ITLFLIIGID LNLANFPDQH LWNAKERIWN QIQEETKSEI QYYEYKGEKL EINPLVTSDN IDSFNLSISY GHFLKYIKVG IIKKVDLYDH GRFAICQMET PQYGTGNRLH TVRVQLPPGS PQVVQTLKQY DVDFTAYSVK QNNNNLFYII AANLLVPVIL ILGLIFLFQN SENFSDGSNP SPMDIGKSPA RFERRPDTGV TFDDVAGIDE AKAEFEEIVS FLKEPEKYKA VGARIPKGIL LSGPPGTGKT MLAKAIANEA DVPFFSVAAS EFVEMFIGIG AARVRDLFRK AAENAPCIVF IDEIDAVGRE RGAGIGGGND EREQTLNQLL TEMDGFRENK GVIVVGATNR IDILDGALLR PGRFDRRIVV GLPDARGRAN ILKVHARNKP LGDDVSLTGL ASNTPGFSGA DLAGLLNEAA ILSTRYGKEI ITLNEINEAT DRISGGISKK PVEKMKNKNL IAYREVGHAV AGSVLKSHDE VERITTKPRG KSKGVTWFAI EEDDNALPSR TEFLARIIST LAGRASERIV FGEAEITTAV GRDLQEATNL ARQMVTRFGM SKIGPMAFED ENSGQVFLGG NMNTGSDYAE NLADRIDNEV RQIIYYCDQK ALEIILDNRI IIDKIARKLT RLDNMDGKTF RKLLCKYTRL PNKYIPYISM FK //