ID   FTSHL_CHLVU             Reviewed;        1720 AA.
AC   P56369;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=ATP-dependent zinc metalloprotease FtsH homolog;
GN   Name=ftsH;
OS   Chlorella vulgaris (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=3077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAM C-27 / Tamiya;
RX   PubMed=9159184; DOI=10.1073/pnas.94.11.5967;
RA   Wakasugi T., Nagai T., Kapoor M., Sugita M., Ito M., Ito S., Tsudzuki J.,
RA   Nakashima K., Tsudzuki T., Suzuki Y., Hamada A., Ohta T., Inamura A.,
RA   Yoshinaga K., Sugiura M.;
RT   "Complete nucleotide sequence of the chloroplast genome from the green alga
RT   Chlorella vulgaris: the existence of genes possibly involved in chloroplast
RT   division.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:5967-5972(1997).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}; Stromal side
CC       {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA57906.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB001684; BAA57905.1; -; Genomic_DNA.
DR   EMBL; AB001684; BAA57906.1; ALT_INIT; Genomic_DNA.
DR   PIR; T07258; T07258.
DR   RefSeq; NP_045830.1; NC_001865.1.
DR   RefSeq; NP_045831.1; NC_001865.1.
DR   AlphaFoldDB; P56369; -.
DR   SMR; P56369; -.
DR   PRIDE; P56369; -.
DR   GeneID; 1457429; -.
DR   GeneID; 809204; -.
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: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; SSF140990; SSF140990; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1720
FT                   /note="ATP-dependent zinc metalloprotease FtsH homolog"
FT                   /id="PRO_0000084662"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1720 AA;  197173 MW;  0F1EA926B799D5BB CRC64;
     MRIEKEIKNL LTTRNFSSEK NQTQFLRIQN WFSTHRLNSR QKNKNSEIKI STFFACLPLA
     LGFSCFLFKK NDIFLEGQGK ASKASSFFQT NLPVFKTYHP KLTFETFEYI VKPTALETQT
     EGSPMIFTPS KKKDFFEKKK NKNDVVLNQN SFFGQPTFVG TIKKSPKPQQ DVLQLVEETL
     FNKSEGISSF LLAENKETVL EQATKKFSGF SCDSYTISSK KLSLVSSSAS KLSKSLSASF
     LKAFMLDEFP SYLQGLNPKS SSFSSDKGVL ITKSPALKVF SKKKYKVEVK SSKVKGQKSE
     SDKHLTFFLE STKLLKKLTL VNSKPSPLIL FKKEAKNDIS NKIVLSPAQK DFSYQTRFSS
     KQPSEKAKAV SVVVKSVKDS NLLDQKTYKN DFLKEKLPLK NKSWKPFLLS KKLSIKTCVE
     NTYYKNQKEF SIDAIQLQAE FQKVFIEKKI SYPFLEEAKA LNPQIKTFEL FNIKNPFLKQ
     CWSIFFQNEM KNRDRNGISG DFTQSILDQE KVQNNELFLD DTSEKILQNL EKVQVWNDSN
     GVRAMSGYIY PDTNTRDLEW FLNLQKTFTR ERVEPFFFQE KRPFKVNSGI KKATAFFPSL
     KKERKNSQLL GVEKTNLSPL EILSKVSFPS RTTNYSFSVK PFPQIFIKTR ESFLTHPETK
     KIIYDGPSVI LDSKKNFDWS TKHQTNLQLW FQKYVSPLNP LVQFQGNFFC EESVEKISQI
     FSSDREKKRE KSEITAFLPL KLGKNAKCEI DWFYDSELVE SFFAPSISSL QIPSEKEQPD
     AFLNQENIRG MYLTLSEPED PNKVEVFFPL LELKQPSFTN SIKQSKRFCH KTSFFENGYS
     SFFEFGVKGN PDFDFSGVFN DQKQFAKKTA SGNYRKTLSF FSKNQEKTSL FVQNWEPLNA
     TSWLAVSQLS FAIFSFRVLK SLSDNYGREL LGYLMDLVAA LGVLDDSLKQ QIQILTGERQ
     TGFRVFLESR KKFTDIVGIQ KVLLELYEIV LFLRNSGRNF THSETLPHGI LLTGPPGTGK
     TLLVQALAGE AQVPVIVLSG SSLMEPGESA AFKLQLVFQE ARQLAPCIVF IDEIDTLSSK
     RSQLLQNPMA NDPGFESFLE SFLLQSKPSQ SVKKTESFFG KFKNGAKKEF DNFKKQKKNP
     AEYNSKQNEK QVSLLSQLLI ELDGIQGRNG VVIFGATNRP EVLDPALLRP GRFDKIVKVG
     LPAQKKRVEI LQFYGQTLGY QKTMPWAYFG ERTVGFTAAD LATLMNESAL KAILNQSNHT
     IETLEHGIER LTTSESEKYT VLKKEKEFKN KTTTPLLNSS RIYSLRLAYY QAGKLLLSYA
     LETHPKTMRA SLWPRRPTLR SLAITANLEK SLFEFARLWE LTERIIGCYA GKAAEFLFLC
     KFSSTGLSEI STLGLEDQVF AQKLVYFMLE NCHFYSKKNA IQQAMKMSPN SNLKELRKKP
     EKLDLYSELL NTIQFPPMWE ASERETSSLT LQKNKEHSGI GFEDQIRYSS PWWQEDVSAE
     MEFKPKNPGK GSRLYLYDYE RTSRNPEWVP PDEFYHNSSG LKDIKNAFVT LSDQKLYSVE
     KATQNKRKEL GKVLAAGFSK KENEGTKNIK KSSAPKASFT KNNVFCEWNE VSKLTRDYPA
     HSLLLQSFNK ALVILNQNRE ILDRIVVELL YQEILKKPQI DDLMKELENS KPKTEPNVFS
     TELQFDASKK APFVELSWGF QSRKPIPRWI DFAAVKGETT