FTSH_SULMD
ID FTSH_SULMD Reviewed; 619 AA.
AC D5D8E3;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=DMIN_00030;
OS Sulcia muelleri (strain DMIN).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Candidatus Sulcia.
OX NCBI_TaxID=641892;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMIN;
RX PubMed=20428247; DOI=10.1371/journal.pone.0010314;
RA Woyke T., Tighe D., Mavromatis K., Clum A., Copeland A., Schackwitz W.,
RA Lapidus A., Wu D., McCutcheon J.P., McDonald B.R., Moran N.A., Bristow J.,
RA Cheng J.F.;
RT "One bacterial cell, one complete genome.";
RL PLoS ONE 5:E10314-E10314(2010).
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: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Cytoplasmic 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; CP001981; ADE35315.1; -; Genomic_DNA.
DR AlphaFoldDB; D5D8E3; -.
DR SMR; D5D8E3; -.
DR PRIDE; D5D8E3; -.
DR EnsemblBacteria; ADE35315; ADE35315; DMIN_00030.
DR KEGG; smh:DMIN_00030; -.
DR HOGENOM; CLU_000688_23_2_10; -.
DR OMA; YDKQGGG; -.
DR Proteomes; UP000008245; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..619
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_5000582995"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 33..131
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 153..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 448
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 224..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 522
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 619 AA; 71722 MW; 862446AAD5AD49C4 CRC64;
MDKQSKFRIK TFFKKIIFFL IIFCFFYFFN FIKKTKKITH TTQDKFFELL SKNKINKFIV
LNKKKVSFTL NEKKSHLDSN NYNFFSKLHL SRYEFEIGDL QLFQKKIDFY KELYEINPNF
EFKNYKIYTV LNFFYDYGFF LMIIIICWIF IFRKIASRSS ESEFKFKIGK SKAKLYYYNN
ITFKDVAGLE GPKEEIKEIV DFLKSPNKYT KLGGKIPKGA LLIGPPGTGK TLLAKAVAGE
AQVPFFSLSG SDFVEMFVGV GASRVRDLFY IAKLKSPSII FIDEIDAIGR ARIKNNIPGG
NDERENTLNK LLTEMDGFST KTNVIVLAAT NRYDVLDDAL LRSGRFDRTI FIDLPSLKER
KDIMKVHLKK IKFSKSIDLD FISRQIPGFS GADISNICNE AALLAARRNK VKVETKDFID
TIYRRIGGIE KKNILIKKNE KKRIAYHETG HAIISWIIEY AHSVFQITIT PRGQSLGAAW
YIPEERQITT EDQMKDEICT LLGGRAAEYL IFNNKSTGAL NDLERITKQA QSMVKFFGLS
SLGNISYFDS TGRNDFSLEK AYSEKTSEII DKEINKIIKE QYKRALEILK KNYDKLIFLA
EKLFKKEVLF KEDFASILD
