FTSH_NOSS1
ID FTSH_NOSS1 Reviewed; 656 AA.
AC Q8YMZ8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=all4776;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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 -!- 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; BA000019; BAB76475.1; -; Genomic_DNA.
DR PIR; AH2402; AH2402.
DR AlphaFoldDB; Q8YMZ8; -.
DR SMR; Q8YMZ8; -.
DR STRING; 103690.17133913; -.
DR MEROPS; M41.017; -.
DR EnsemblBacteria; BAB76475; BAB76475; BAB76475.
DR KEGG; ana:all4776; -.
DR eggNOG; COG0465; Bacteria.
DR OMA; QVMQFGQ; -.
DR Proteomes; UP000002483; 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: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; IEA:InterPro.
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; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Nucleotide-binding; Protease; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..656
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400323"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 67..147
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 169..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 461
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 656 AA; 72152 MW; 5E754428DB5E5115 CRC64;
MAIFARRIGL NQHSAYGSRQ RVIVMKNFGK KALIKQQSPK RVAWTGALAA SLIMLPTMFG
GNPVLAQKAE RESLSYGELI QKVNQEQVKR VELDETEQIA KVYLKGQKPD APPIQVRLLE
QNNELINRLK EKNVDFGEIS SANSRAAVGL LINLMWILPL VALMLLFLRR STNASSQAMN
FGKSRARFQM EAKTGVKFDD VAGIEEAKEE LQEVVTFLKQ PERFTAVGAR IPKGVLLVGP
PGTGKTLLAK AIAGEAAVPF FSISGSEFVE MFVGVGASRV RDLFKKAKDN APCLIFIDEI
DAVGRQRGTG IGGGNDEREQ TLNQLLTEMD GFEGNTGIII IAATNRPDVL DSALLRPGRF
DRQVIVDAPD LKGRLEILQV HSRNKKVDPS VSLEAIARRT PGFTGADLAN LLNEAAILTA
RRRKEAITIL EIDDAVDRVV AGMEGTPLVD SKSKRLIAYH EVGHGLVGTL LKDHDPVQKV
TLIPRGQAQG LTWFTPNEEQ GLISRSQLKA RITSTLAGRA AEEIVFGKPE VTTGAGDDLQ
KVTSMARQMV TKFGMSELGP LSLENQSGEV FLGRDWMNKS DYSEEIAAKI DSQVREIINT
CYQTSKELLQ TNRVVMERLV DLLTEQETIE GDLFRKIVSE SQNPVVDEQL SMVNSQ
