FTSH4_SYNY3
ID FTSH4_SYNY3 Reviewed; 628 AA.
AC P73437;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 4 {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH4 {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=sll1463;
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: No visible phenotype.
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; BAA17477.1; -; Genomic_DNA.
DR PIR; S77374; S77374.
DR AlphaFoldDB; P73437; -.
DR SMR; P73437; -.
DR IntAct; P73437; 5.
DR STRING; 1148.1652556; -.
DR MEROPS; M41.021; -.
DR PaxDb; P73437; -.
DR EnsemblBacteria; BAA17477; BAA17477; BAA17477.
DR KEGG; syn:sll1463; -.
DR eggNOG; COG0465; Bacteria.
DR InParanoid; P73437; -.
DR OMA; YDKQGGG; -.
DR PhylomeDB; P73437; -.
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 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..628
FT /note="ATP-dependent zinc metalloprotease FtsH 4"
FT /id="PRO_0000084654"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 36..119
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 141..628
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 439
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 214..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 628 AA; 68199 MW; 8BE2563000F73EBA CRC64;
MAIKPQPQWQ RRLASVLLWG STIYLLVNLL APALFRSQPP QVPYSLFIDQ VEGDKVASVY
VGQNEIRYQL KPEAEDEGKE KAAEGQILRT TPIFDLELPK RLEAKGIEFA AAPPAKNSWF
GTLLSWVIPP LIFVGIWSFF LNRNNNGAPG GALAFTKSKA KVYVEGDSTK VTFDDVAGVE
EAKTELSEVV DFLKFPQRYT ALGAKIPKGV LLVGPPGTGK TLLAKAAAGE AGVPFFIISG
SEFVELFVGA GAARVRDLFE QAKKQAPCIV FIDELDAIGK SRASGAFMGG NDEREQTLNQ
LLTEMDGFSA AGATVIVLAA TNRPETLDPA LLRPGRFDRQ VLVDRPDLAG RLKILEIYAK
KIKLDKEVEL KNIATRTPGF AGADLANLVN EAALLAARNK QDSVTEADFR EAIERVVAGL
EKKSRVLSDK EKKIVAYHEV GHALVGAVMP GGGQVAKISI VPRGMAALGY TLQMPTEDRF
LLNESELRDQ IATLLGGRAA EEIVFDSITT GAANDLQRAT DLAEQMVTTY GMSKVLGPLA
YDKGQQNNFL GQGMGNPRRM VSDDTAKEID LEVKEIVEQG HNQALAILEH NRDLLEAIAE
KILEKEVIEG EELHHLLGQV QAPGTLVV
