FTSH2_SYNY3
ID FTSH2_SYNY3 Reviewed; 627 AA.
AC Q55700;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 2;
DE EC=3.4.24.-;
GN Name=ftsH2; OrderedLocusNames=slr0228;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-14, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12069591; DOI=10.1021/bi026012+;
RA Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K.,
RA Pakrasi H.B.;
RT "Proteomic analysis of a highly active photosystem II preparation from the
RT cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel
RT polypeptides.";
RL Biochemistry 41:8004-8012(2002).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=10940391; DOI=10.1016/s0014-5793(00)01871-8;
RA Mann N.H., Novac N., Mullineaux C.W., Newman J., Bailey S., Robinson C.;
RT "Involvement of an FtsH homologue in the assembly of functional photosystem
RT I in the cyanobacterium Synechocystis sp. PCC 6803.";
RL FEBS Lett. 479:72-77(2000).
RN [5]
RP FUNCTION IN PSII REPAIR AND D1 TURNOVER, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12953117; DOI=10.1105/tpc.012609;
RA Silva P., Thompson E., Bailey S., Kruse O., Mullineaux C.W., Robinson C.,
RA Mann N.H., Nixon P.J.;
RT "FtsH is involved in the early stages of repair of photosystem II in
RT Synechocystis sp PCC 6803.";
RL Plant Cell 15:2152-2164(2003).
RN [6]
RP PSBB (CP47) AND D2 AS SUBSTRATES, AND LACK OF LOCALIZATION TO THE CELL
RP INNER MEMBRANE.
RX PubMed=16286465; DOI=10.1074/jbc.m503852200;
RA Komenda J., Barker M., Kuvikova S., de Vries R., Mullineaux C.W., Tichy M.,
RA Nixon P.J.;
RT "The FtsH protease slr0228 is important for quality control of photosystem
RT II in the thylakoid membrane of Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 281:1145-1151(2006).
RN [7]
RP ROLE IN REPAIR FOLLOWING UV-B INDUCED DAMAGE, D2 AS SUBSTRATE, AND
RP INDUCTION.
RX PubMed=17208194; DOI=10.1016/j.bbabio.2006.11.016;
RA Cheregi O., Sicora C., Kos P.B., Barker M., Nixon P.J., Vass I.;
RT "The role of the FtsH and Deg proteases in the repair of UV-B radiation-
RT damaged Photosystem II in the cyanobacterium Synechocystis PCC 6803.";
RL Biochim. Biophys. Acta 1767:820-828(2007).
RN [8]
RP GGPS AS SUBSTRATE, AND DISRUPTION PHENOTYPE.
RX PubMed=17116240; DOI=10.1111/j.1365-2958.2006.05495.x;
RA Stirnberg M., Fulda S., Huckauf J., Hagemann M., Kramer R., Marin K.;
RT "A membrane-bound FtsH protease is involved in osmoregulation in
RT Synechocystis sp. PCC 6803: the compatible solute synthesizing enzyme GgpS
RT is one of the targets for proteolysis.";
RL Mol. Microbiol. 63:86-102(2007).
RN [9]
RP INTERACTION WITH FTSH3 AND PSII, AND INDUCTION BY OXIDATIVE STRESS.
RX PubMed=17635189; DOI=10.1111/j.1365-2958.2007.05822.x;
RA Zhang P., Sicora C.I., Vorontsova N., Allahverdiyeva Y., Battchikova N.,
RA Nixon P.J., Aro E.M.;
RT "FtsH protease is required for induction of inorganic carbon acquisition
RT complexes in Synechocystis sp. PCC 6803.";
RL Mol. Microbiol. 65:728-740(2007).
RN [10]
RP POSSIBLE MECHANISM OF SUBSTRATE RECOGNITION.
RX PubMed=17905897; DOI=10.1105/tpc.107.053868;
RA Komenda J., Tichy M., Prasil O., Knoppova J., Kuvikova S., de Vries R.,
RA Nixon P.J.;
RT "The exposed N-terminal tail of the D1 subunit is required for rapid D1
RT degradation during photosystem II repair in Synechocystis sp PCC 6803.";
RL Plant Cell 19:2839-2854(2007).
RN [11]
RP INTERACTION WITH YIDC, AND SUBUNIT.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=30061392; DOI=10.1073/pnas.1800609115;
RA Yu J., Knoppova J., Michoux F., Bialek W., Cota E., Shukla M.K.,
RA Straskova A., Pascual Aznar G., Sobotka R., Komenda J., Murray J.W.,
RA Nixon P.J.;
RT "Ycf48 involved in the biogenesis of the oxygen-evolving photosystem II
RT complex is a seven-bladed beta-propeller protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E7824-E7833(2018).
RN [12]
RP REVIEW.
RX PubMed=20338950; DOI=10.1093/aob/mcq059;
RA Nixon P.J., Michoux F., Yu J., Boehm M., Komenda J.;
RT "Recent advances in understanding the assembly and repair of photosystem
RT II.";
RL Ann. Bot. 106:1-16(2010).
CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for
CC both cytoplasmic and membrane proteins. Plays a role in the quality
CC control of integral membrane proteins (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Plays a role in the selective replacement of photosystem II
CC (PSII) protein D1 in the PSII repair cycle following visible-light and
CC UV-B induced damage. If damaged D1 is not removed then new D1 cannot be
CC inserted to restore the PSII reaction center. Seems to also degrade
CC damaged and/or unassembled PSII proteins D2 and PsbB (CP47). May
CC recognize D1 via its first 20 amino acids, as deletion of these
CC prevents the PSII repair cycle. Also seems to degrade cytoplasmic GGPS,
CC glucosylglycerol-phosphate synthase. {ECO:0000269|PubMed:12953117,
CC ECO:0000269|PubMed:17208194}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homohexamer (Potential). Part of a large (>500 kDa) complex
CC that includes FtsH3 and PSII. Coimmunoprecipitates with YidC
CC (PubMed:30061392). {ECO:0000269|PubMed:12953117,
CC ECO:0000269|PubMed:30061392, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:12953117}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12069591,
CC ECO:0000269|PubMed:12953117}; Stromal side
CC {ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:12953117}. Note=A
CC fraction is found associated with PSII. Localization to the cell inner
CC membrane has been specifically tested and not seen.
CC -!- INDUCTION: By UV-B light and oxidative stress provided by methyl
CC viologen. {ECO:0000269|PubMed:17208194, ECO:0000269|PubMed:17635189}.
CC -!- DISRUPTION PHENOTYPE: Cells have decreased chlorophyll content, with a
CC 60% reduction in the content of photosystem I (PSI). The PSI that
CC remains may have an altered structure. Cells grow normally under very
CC low light (10 umol photons/m(2)/s) but are dramatically inhibited by
CC low light at 40 umol photons/m(2)/s. Under this light intensity they
CC also photobleach. Reduced rates of D1 processing and degradation are
CC observed. Mutants show increased tolerance for non-ionic stress by
CC maltose but also an increased sensitivity to high NaCl concentrations.
CC {ECO:0000269|PubMed:10940391, ECO:0000269|PubMed:17116240}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10230.1; -; Genomic_DNA.
DR PIR; S76378; S76378.
DR AlphaFoldDB; Q55700; -.
DR SMR; Q55700; -.
DR IntAct; Q55700; 2.
DR STRING; 1148.1001602; -.
DR MEROPS; M41.017; -.
DR PaxDb; Q55700; -.
DR EnsemblBacteria; BAA10230; BAA10230; BAA10230.
DR KEGG; syn:slr0228; -.
DR eggNOG; COG0465; Bacteria.
DR InParanoid; Q55700; -.
DR OMA; QVMQFGQ; -.
DR PhylomeDB; Q55700; -.
DR BRENDA; 3.4.24.B20; 382.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; IBA:GO_Central.
DR GO; GO:0042651; C:thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010206; P:photosystem II repair; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR011546; Pept_M41_FtsH_extracell.
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; PF06480; FtsH_ext; 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 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Protease; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..627
FT /note="ATP-dependent zinc metalloprotease FtsH 2"
FT /id="PRO_0000084652"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..117
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 434
FT /evidence="ECO:0000250"
FT BINDING 212..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 627 AA; 68496 MW; 4B2C160213CD0517 CRC64;
MKFSWRTALL WSLPLLVVGF FFWQGSFGGA DANLGSNTAN TRMTYGRFLE YVDAGRITSV
DLYENGRTAI VQVSDPEVDR TLRSRVDLPT NAPELIARLR DSNIRLDSHP VRNNGMVWGF
VGNLIFPVLL IASLFFLFRR SSNMPGGPGQ AMNFGKSKAR FQMDAKTGVM FDDVAGIDEA
KEELQEVVTF LKQPERFTAV GAKIPKGVLL VGPPGTGKTL LAKAIAGEAG VPFFSISGSE
FVEMFVGVGA SRVRDLFKKA KENAPCLIFI DEIDAVGRQR GAGIGGGNDE REQTLNQLLT
EMDGFEGNTG IIIIAATNRP DVLDSALMRP GRFDRQVMVD APDYSGRKEI LEVHARNKKL
APEVSIDSIA RRTPGFSGAD LANLLNEAAI LTARRRKSAI TLLEIDDAVD RVVAGMEGTP
LVDSKSKRLI AYHEVGHAIV GTLLKDHDPV QKVTLIPRGQ AQGLTWFTPN EEQGLTTKAQ
LMARIAGAMG GRAAEEEVFG DDEVTTGAGG DLQQVTEMAR QMVTRFGMSN LGPISLESSG
GEVFLGGGLM NRSEYSEEVA TRIDAQVRQL AEQGHQMARK IVQEQREVVD RLVDLLIEKE
TIDGEEFRQI VAEYAEVPVK EQLIPQL
