FTSH1_SYNY3
ID FTSH1_SYNY3 Reviewed; 665 AA.
AC P73179;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 1 {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH1 {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=slr1390;
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 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).
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. {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- INDUCTION: Slight induction by UV-B light.
CC {ECO:0000269|PubMed:17208194}.
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; BAA17205.1; -; Genomic_DNA.
DR PIR; S75291; S75291.
DR AlphaFoldDB; P73179; -.
DR SMR; P73179; -.
DR IntAct; P73179; 1.
DR STRING; 1148.1652282; -.
DR MEROPS; M41.017; -.
DR MEROPS; M41.021; -.
DR PaxDb; P73179; -.
DR PRIDE; P73179; -.
DR EnsemblBacteria; BAA17205; BAA17205; BAA17205.
DR KEGG; syn:slr1390; -.
DR eggNOG; COG0465; Bacteria.
DR InParanoid; P73179; -.
DR OMA; TLCPGHD; -.
DR PhylomeDB; P73179; -.
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; 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 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Nucleotide-binding; Protease; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..665
FT /note="ATP-dependent zinc metalloprotease FtsH 1"
FT /id="PRO_0000084653"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 43..159
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 181..665
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 41..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 473
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 251..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 472
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 476
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 665 AA; 72110 MW; D61680D321A728A8 CRC64;
MSHRPRSDRH SFSSPSRFWH RLGMGLLVAG TLALPVSTLA QEGGEGAQPK ASPSPIQSPN
SSNGEATPRS FFNSGSPRSA EPKMNYGQLI DAIKANQVAK VEVDTNRRQA IVTLKDAPPG
SKPQTVQLLD NNPELLNLLR SRSETIDLDI NRTPDNSALY GLLTNLLVVA ILIGLVVMVV
RRSANASGQA MSFGKSKARF QMEAKTGVGF DDVAGIDEAK EELQEVVTFL KQPEKFTAIG
AKIPRGVLLI GPPGTGKTLL AKAIAGEAGV PFFSISGSEF VEMFVGVGAS RVRDLFKKAK
ENAPCLVFID EIDAVGRQRG VGYGGGNDER EQTLNQLLTE MDGFEGNSGI IVIAATNRPD
VLDLALLRPG RFDRQVTVDY PDVQGRELIL AIHAQNKKLH EEVQLAAIAR RTPGFTGADL
ANVLNEAAIF TARRRKEAIT MAEVNDAIDR VVAGMEGTPL VDSKSKRLIA YHEVGHALIG
TLCPGHDPVE KVTLIPRGQA QGLTWFTPDE DQSLMTRNQM IARIAGLLGG RVAEEVIFGD
DEVTTGAGND IEKITYLARQ MVTKLGMSSL GLVALEEEGD RNFSGGDWGK RSEYSEDIAA
RIDREIQAIV TAAHQRATRI IEENRNLMDL LVDALIDQET IEGEHFRQLV ESYQQSQKQP
ALAGK
