FTSH_ZYMMN
ID FTSH_ZYMMN Reviewed; 662 AA.
AC C8WEG0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=Za10_1558;
OS Zymomonas mobilis subsp. mobilis (strain NCIMB 11163 / B70).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=622759;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11163 / B70;
RX PubMed=19767433; DOI=10.1128/jb.01084-09;
RA Kouvelis V.N., Saunders E., Brettin T.S., Bruce D., Detter C., Han C.,
RA Typas M.A., Pappas K.M.;
RT "Complete genome sequence of the ethanol producer Zymomonas mobilis NCIMB
RT 11163.";
RL J. Bacteriol. 191:7140-7141(2009).
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; CP001722; ACV76096.1; -; Genomic_DNA.
DR AlphaFoldDB; C8WEG0; -.
DR SMR; C8WEG0; -.
DR MEROPS; M41.001; -.
DR KEGG; zmn:Za10_1558; -.
DR HOGENOM; CLU_000688_16_0_5; -.
DR OMA; YDKQGGG; -.
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..662
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400418"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 49..126
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 148..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 641..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 219..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 662 AA; 72350 MW; 43743E1F47739436 CRC64;
MKGLIYYMAM NDNNKTPQDP QANNWMKTLL IGGGIIAAMT LAVTFFDGNG GRDHNTTSVA
YSEFLNRVDN NGVKDVTIGH DELSGHFTDN SAFKTVAPSD PLLVQRLQSK NVTFRALPED
TVSFWQILLS QFLLPFILFV GLGFLFVRQM QKNGGGGAMG FGKSRARLLT EKQGRVTFKD
IAGIEEAREE LEEIVDFLKD PTRFSRLGGK IPKGALLVGP PGTGKTLLAR AIAGEAGVPF
FSISGSDFVE MFVGVGASRV RDMFEQAKKN APCIIFIDEI DAVGRHRGAG LGNGNDEREQ
TLNQLLVEMD GFEANEGIII LAATNRPDVL DPALLRPGRF DRQVIVPRPD IEGRLKILQV
HMKKTPLAPD VDVRTIARGT PGFSGADLAN IVNEAALLAA RKGKRLVAMS EFEEAKDKVM
MGAERRSVIM TEEEKRSTAY HEAGHALVSL HIPGCDPLHK VTVIPRGRAL GVTWNLPERD
QLSINIKQMK ARLALCFGGR IAEQLVYGED SLNTGASNDI QQATDMARAM VTEYGMSPKL
GWLRYRENQD EVFLGHSVSR SQNISEDTAK IIDQEVRVLV EEGESRARQV LTEHIDELHR
LANALIEYET LSGEEAKRAI AGEKITTIEV KPQVTIPLSG GASGVPKSPP FNGWGNAAPQ
GA
