ID   FTSHL_OLTVI             Reviewed;        2292 AA.
AC   Q20EZ8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=ATP-dependent zinc metalloprotease FtsH homolog;
GN   Name=ftsH;
OS   Oltmannsiellopsis viridis (Marine flagellate) (Oltmannsiella viridis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; Oltmannsiellopsidales;
OC   Oltmannsiellopsidaceae; Oltmannsiellopsis.
OX   NCBI_TaxID=51324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16472375; DOI=10.1186/1741-7007-4-3;
RA   Pombert J.-F., Lemieux C., Turmel M.;
RT   "The complete chloroplast DNA sequence of the green alga Oltmannsiellopsis
RT   viridis reveals a distinctive quadripartite architecture in the chloroplast
RT   genome of early diverging ulvophytes.";
RL   BMC Biol. 4:3-3(2006).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- DOMAIN: Lacks the zinc protease domain of other FtsH proteins. Also
CC       much longer in both the N- and C-termini.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; DQ291132; ABB82008.1; -; Genomic_DNA.
DR   RefSeq; YP_635847.1; NC_008099.1.
DR   AlphaFoldDB; Q20EZ8; -.
DR   SMR; Q20EZ8; -.
DR   PRIDE; Q20EZ8; -.
DR   GeneID; 4100186; -.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:InterPro.
DR   Gene3D; 1.20.58.760; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   Pfam; PF00004; AAA; 2.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; Plastid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..2292
FT                   /note="ATP-dependent zinc metalloprotease FtsH homolog"
FT                   /id="PRO_0000293974"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          117..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          814..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1652..1678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..887
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1435..1452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1468..1494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1652..1670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2292 AA;  257727 MW;  0B888D64B3B6B45E CRC64;
     MTQLSSSQPI GETFTIWKFT FFKFYFGILD HREQTKNLFL NYSTKYISFE FLCCCFPFFI
     GLTQLVLLRY QNQFTSEVLQ KTIPGLGSSY QPISWETFSY LNYKSYLSEG EAPHPFNKEG
     SLSKNSASSE RREPNLMGLS PLYNTPQIDV YSDSIIITPP QKLDFSSAAN SQSLLGWGDQ
     QNPLIVGEIK SQKPTGYLSE VVEKKWILPS RNAVIFYKTN SSHGKDIQKL KIKKPLGSLR
     LEIFGRKSPY GLDLFPKKLN PIYAKLNPST LPDGGKVSVG LFSESSARTG DSTVFKSTLN
     PAGVVKKEES KSLQGFLKLS KKNFDPLNYQ QRTQVQQAVF DSLLYNQGLL VNNASRPIKL
     KPKANSFLDT TFDLIRSKKQ KLSAKKTGGF AIPENSNKKV ECSNSKLQNY NLLERYTLWK
     NYKAQTNERN TRAFNEQQSF LFDSNNGSVK KESNQYSTQA PQHGPSPNTP KGVLRDGSVG
     GGWKSLTKVH SLLTQWNYVQ KRNNLTSRLM SGYNYPDVTN DGVKALNSSL TSFLSSGSRS
     PFGDTLRRPA TNQSQRLSRM LPLKIHLPGN STSAITYPVP ATGWTTSPQH SFRSVGGNAF
     TDKLSRANDS QPAPQHLSPN TPKGVLRDGS VGGENQKEQE KQQNSGSLYQ TTRGRSFGNP
     FSTQLVFLQR VLETDKNESQ TDSEASSAML RPQHFGSIGE RSGLSQTTLN GGNQFKQTEG
     TLLNQIRKDS FTLSYQNAKK PTNWSRKTKA YVLLDCETND LTPEQTLSTK PAFEGEALRP
     SDLKLWLKTY LSSDNPALKH KSTFFSTDTT KTPMLTELKA TPDGRSTPKG SPEGARDLAI
     SNQPSNTQKT KEKNSSHWST EGRSTPSSLQ VTKSLKVIET PTQTDANGQQ IDLNRETRRW
     SIPGYQTWQI PLIDKHSSLF LLERLEPKLY KKITEFLTND SKLSFNASQK VGPTGLPAEK
     EKVSERVLQE SFTRNVLPLT EVRYPTNSVF MGNRNQSQNV LATENEYPAS FFDLKSLSFF
     LENKTKKVNQ SVVAEGHSVG RLVYNKKINF RSSPKINFHY LPVVEGPVYG ATQNTLQVAG
     TYSKTTSVYK HLTTKSNQSS STINQSRSEV PTNRVETWEP LTPFSWLIVT QLSFGLISLK
     VLQNLYQDYG KELISYVLDL LSIFGDSVEA SLDESLKEEF QAQQDGSGAR LIRKVDKRFQ
     NLAGIQRILP ECSEIVWFLR NYSFMKSSGL VYLSPVDREN RCVKDALHWI QDFPEHFSST
     SLHIEEEGYP VDVISKNFAK GNKIVSTLQE GGTTKSNKIQ FGHSKRYSLS LVSQNLTALA
     LAPSNWLTFE KMIPKGILLV GPPGTGKTLL VQAIAGEANV PVLVQSLSLI SQPGESDSGA
     EKLTDLFKRA RELSPCIVFI DEIDTLGIKR QNLIQNPMGT DNLLNCLYPK NSGQQLSMTD
     GSKSSTVRTT TRLGKECPFP PHTTRSFGLD TNKDEMETRS SESTKASHES SNEMEVEKNQ
     LSALIRLLVE MDGLNPLNGV IVFGATNRPE VLDPALIRPG RFDQILPIEL PGKQKRVEIL
     KLYAKKLGTA KSISWEYFAN RTVGLSAADL AAIMNQSTIL AVFNDQRHTL KTLEYGLNII
     YKPKTGPILT KKVQGELNSS LADKSSNWTV DKKASTTSKS SLTSTPQHFH GSVGGEYPPK
     QVVVGTPGTT LLKQQLELEK NVLFKKGLEP KSQKLEIVTP IQQQSLVSEK LDLLKKKTYK
     KNISQLKLKT LNKLEKLSVQ SLNTKTPQHF QGLMGGVSQR EGNFTESLFS EKVTYTLSQL
     VQTWPKVLTS SKLKQKTPQY NEVLSSESLN KKIWVSSDTT HPYSVQKQFL TYVSVKKGFG
     STLDVSMSLP ELTVEKWLSS DSTYATDPFT LNRFGYYQSG KVLTQCLVEK IDSKTLEVSE
     TSQSLKTDVS KSGLLNNKQK TSPSGLLFDS ACNTLDSQTQ QLKTPKLTHF TRLESYFDTA
     EATPVVLNLF PRFKNVRYQD ESLRGKTEQK GNRSNPLSLA SFEKQLISLL AGKASEILFF
     ATRSVNVTKK GNSLHRGETG SQNSNFSASN WDSNLGVDLK FANKMANAMV NQWYFYSKKV
     LTRKTNQLAL NHNTQEFNQK ETIKFFQELT NQVENEMSYS VKAYKTGYFR NFQASSGKPW
     WQVKVAQQVG NLESAYTDWY RIYLPDTEES ERNQEWTPPD QFFQNVERLA RLNNKLENFT
     LDSEITWNDL GKMDRDFLYQ SLLLNSFNQA FQVLDISRPL LDYFTDYLIR YEIMRQDTIN
     KCLLNYEKFT DS