ID A0A3N6P0W9_9CYAN Unreviewed; 613 AA.
AC A0A3N6P0W9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458};
GN Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
GN ORFNames=D5R40_07515 {ECO:0000313|EMBL:RQH49059.1};
OS Okeania hirsuta.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Okeania.
OX NCBI_TaxID=1458930 {ECO:0000313|EMBL:RQH49059.1, ECO:0000313|Proteomes:UP000269154};
RN [1] {ECO:0000313|EMBL:RQH49059.1, ECO:0000313|Proteomes:UP000269154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAB10Feb10-1 {ECO:0000313|EMBL:RQH49059.1,
RC ECO:0000313|Proteomes:UP000269154};
RX PubMed=30444349;
RA Moss N.A., Leao T., Rankin M., McCullough T.M., Qu P., Korobeynikov A.,
RA Smith J.L., Gerwick L., Gerwick W.H.;
RT "Ketoreductase domain dysfunction expands chemodiversity: malyngamide
RT biosynthesis in the cyanobacterium Okeania hirsuta.";
RL ACS Chem. Biol. 0:0-0(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:0000256|HAMAP-
CC Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01458};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01458};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01458}; Stromal side {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044, ECO:0000256|HAMAP-
CC Rule:MF_01458}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQH49059.1}.
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DR EMBL; RCBY01000028; RQH49059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6P0W9; -.
DR OrthoDB; 548807at2; -.
DR Proteomes; UP000269154; Unassembled WGS sequence.
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 CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.720.210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 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 NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
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; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01458};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01458};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458};
KW Reference proteome {ECO:0000313|Proteomes:UP000269154};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01458};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01458}; Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 190..329
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT ACT_SITE 421
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 613 AA; 67074 MW; 39B0F0B31AB6D924 CRC64;
MNNKRWRNAG LYALLAIVVI ALATAFFDQQ PQTSETWKYS QFIQQVETKN VDRVSISADR
TAARVKVADG SIVRVNLPND PDLINILTKN NVDISVLPQS EEGFWVRALS SLFFPVLLLV
GLFFLLRRAQ SGPGSQAMNF GKSKARVQME PQTQVTFGDV AGIEQAKLEL TEVVDFLKNA
DRFTAVGAKI PKGVLLVGPP GTGKTLLAKA VAGEAGVPFF SISGSEFVEM FVGVGASRVR
DLFEQAKSNA PCIVFIDEID AVGRQRGAGL GGGNDEREQT LNQLLTEMDG FEGNTGIIII
AATNRPDVLD AALLRPGRFD RQVVVDRPDY AGRLEILNVH ARGKSLSKDV DLEKIARRTP
GFTGADLSNL LNEGAILAAR RNLTEISMDE VNDAIDRVLA GPEKKDRVMS EKRKELVAYH
EAGHALVGAL MPDYDPVQKI SIIPRGRAGG LTWFTPSEDR MDSGLYSRAY LQNQMAVALG
GRLAEEIIFG DEEVTTGASN DLQQVANVAR QMVTRFGMSD RLGPVALGRQ NGNMFLGRDI
MAERDFSEET AAAIDDEVRN LVEQAYRRAK EVLVSNRHIL DKLAEMLVDK ETVDSDELQE
LLATNDVKMA ALI
//
