FTSH_CLONN
ID FTSH_CLONN Reviewed; 676 AA.
AC A0PXM8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=NT01CX_1040;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01458};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458};
CC 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; CP000382; ABK60661.1; -; Genomic_DNA.
DR RefSeq; WP_011721151.1; NC_008593.1.
DR AlphaFoldDB; A0PXM8; -.
DR SMR; A0PXM8; -.
DR STRING; 386415.NT01CX_1040; -.
DR MEROPS; M41.009; -.
DR EnsemblBacteria; ABK60661; ABK60661; NT01CX_1040.
DR KEGG; cno:NT01CX_1040; -.
DR PATRIC; fig|386415.7.peg.156; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_9; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000008220; 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 membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..676
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400336"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 31..112
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 134..676
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 650..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 431
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 676 AA; 74487 MW; 9280D66335A3F3CC CRC64;
MGGINVKKRL SSATIWIVLL IVLFFAAITV LESSKTSGAI SYNEFKKYWI ENKVSRVEIK
QDGRTVAGEL NDKAKTQFQV VVPQSLLVQD ILVNNPKSSV NVKFEPASSM PMWISWIPTI
ILILVMVGFW VMFMQQSQGG GGGNRGVMNF GKSRAKLATP DSQKVTFKDV AGADEEKGEL
EEIVDFLKEP KKYLDMGARI PKGILLVGPP GTGKTLLAKA VAGEAGVPFF SISGSDFVEM
FVGVGASRVR DLFEQAKKNS PCIIFIDEID AVGRQRGAGL GGGHDEREQT LNQLLVEMDG
FGVNEGIILV AATNRPDILD KALLRPGRFD RQILVGAPDA KGREEVLKVH VRNKRLSDDV
DLKVLAKRTP GFVGADLENL MNEAALLAVR ANKKQIGMEE LEEAITRVIA GPEKKSRVIH
EEDRKITAYH EAGHAIVMKF SPHSDPVHEI SIIPRGMAGG YTMHLPERDT SYMSKSKLKD
EMVGLLGGRV AEQIIIGDIS TGASNDIQRV SNIARKMVME YGMSEKLGTI TFGSDHDEVF
IGREIGKSKN YSEEVAFEID NEVKALVDEA YKKAEKILTE HIDKLHAVAK VLLDKEKVTG
EEFNAIVEGR PLEELNKKEN AIDLEKHDNV EEVHDDVEGV HDDVEGVNIK DTSEDNIETT
DAFANNTDLE EDKKEI
