FTSH3_SYNY3
ID FTSH3_SYNY3 Reviewed; 616 AA.
AC P72991;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 3 {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH3 {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=slr1604;
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=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 [2]
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 [3]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS 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 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 [5]
RP INTERACTION WITH FTSH2 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 [6]
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).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01458};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458};
CC -!- SUBUNIT: Homohexamer (Potential). Part of a large complex that includes
CC FtsH2 and PSII. Coimmunoprecipitates with YidC (PubMed:30061392).
CC {ECO:0000255|HAMAP-Rule:MF_01458, ECO:0000269|PubMed:30061392}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01458, ECO:0000269|PubMed:12069591}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01458, ECO:0000269|PubMed:12069591};
CC Stromal side {ECO:0000255|HAMAP-Rule:MF_01458,
CC ECO:0000269|PubMed:12069591}. Note=Some is found associated with
CC photosystem II.
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: A homozygous disruption strain was not
CC identified, suggesting this gene may be essential.
CC {ECO:0000269|PubMed:10940391}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000255|HAMAP-Rule:MF_01458}.
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DR EMBL; BA000022; BAA17010.1; -; Genomic_DNA.
DR PIR; S74970; S74970.
DR AlphaFoldDB; P72991; -.
DR SMR; P72991; -.
DR IntAct; P72991; 8.
DR STRING; 1148.1652085; -.
DR MEROPS; M41.024; -.
DR PaxDb; P72991; -.
DR PRIDE; P72991; -.
DR EnsemblBacteria; BAA17010; BAA17010; BAA17010.
DR KEGG; syn:slr1604; -.
DR eggNOG; COG0465; Bacteria.
DR InParanoid; P72991; -.
DR OMA; QYGMTER; -.
DR PhylomeDB; P72991; -.
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:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009579; C:thylakoid; IBA:GO_Central.
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: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; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Nucleotide-binding; Protease; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..616
FT /note="ATP-dependent zinc metalloprotease FtsH 3"
FT /id="PRO_0000084655"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 31..108
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 130..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 424
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 201..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 616 AA; 67250 MW; 878D0F5F9107B3EC CRC64;
MSKNNKKWRN AGLYALLLIV VLALASAFFD RPTQTRETLS YSDFVNRVEA NQIERVNLSA
DRTQAQVPNP SGGPPYLVNL PNDPDLINIL TQHNVDIAVQ PQSDEGFWFR IASTLFLPIL
LLVGIFFLFR RAQSGPGSQA MNFGKSKARV QMEPQTQVTF GDVAGIEQAK LELTEVVDFL
KNADRFTELG AKIPKGVLLV GPPGTGKTLL AKAVAGEAGV PFFSISGSEF VEMFVGVGAS
RVRDLFEQAK ANAPCIVFID EIDAVGRQRG AGLGGGNDER EQTLNQLLTE MDGFEGNTGI
IIVAATNRPD VLDSALMRPG RFDRQVVVDR PDYAGRREIL NVHARGKTLS QDVDLDKIAR
RTPGFTGADL SNLLNEAAIL AARRNLTEIS MDEVNDAIDR VLAGPEKKNR VMSEKRKTLV
AYHEAGHALV GALMPDYDPV QKISIIPRGR AGGLTWFTPS EDRMESGLYS RSYLQNQMAV
ALGGRIAEEI IFGEEEVTTG ASNDLQQVAR VARQMVTRFG MSDRLGPVAL GRQGGGVFLG
RDIASDRDFS DETAAAIDEE VSQLVDQAYQ RAKQVLVENR GILDQLAEIL VEKETVDSEE
LQTLLANNNA KLALLV
