FTSH_MYCGH
ID FTSH_MYCGH Reviewed; 765 AA.
AC D3FFN2;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=MGAH_0659;
OS Mycoplasma gallisepticum (strain R(high / passage 156)) (Mycoplasmoides
OS gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710128;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(high / passage 156);
RX PubMed=20123709; DOI=10.1128/iai.01172-09;
RA Szczepanek S.M., Tulman E.R., Gorton T.S., Liao X., Lu Z., Zinski J.,
RA Aziz F., Frasca S. Jr., Kutish G.F., Geary S.J.;
RT "Comparative genomic analyses of attenuated strains of Mycoplasma
RT gallisepticum.";
RL Infect. Immun. 78:1760-1771(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 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; CP001872; ADC30208.1; -; Genomic_DNA.
DR RefSeq; WP_011113255.1; NC_017502.1.
DR AlphaFoldDB; D3FFN2; -.
DR SMR; D3FFN2; -.
DR PRIDE; D3FFN2; -.
DR GeneID; 57203303; -.
DR KEGG; mgh:MGAH_0659; -.
DR PATRIC; fig|710128.3.peg.30; -.
DR HOGENOM; CLU_000688_16_2_14; -.
DR OMA; QYGMTER; -.
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; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..765
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400359"
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..213
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 235..765
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 730..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 537
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 314..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 540
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 765 AA; 82881 MW; 627FF098E6BABD2A CRC64;
MSNTSNFNER VTENAKPPKN VKSIIWKTIG IIIVMAIIIG LILFYVLPRN TIANISNIQY
VDGNLVATAT INGRSGRFIL DLENSTYQTS YTSGLSLSIS VFLRNLNNAN GQSFFVSLIR
PATSSANDAV FNIANLSINQ TRGVATLVTE GGSYSAVLTT TLTALPLTGQ KFLPEGFNLD
TANTDAYRAA GAIPGIQRLL AVGNVQLPNQ STAILTQFLT SIIPFVILIV IYIVIARRFS
RTMGAGGAIG EDGENVFTIG KSQAKLAKST FKFTDVAGIE EEKSELIELV DYLKRPGKYV
QMGARTPRGV VLYGPPGTGK TLLAKAVAGE AGVPFFQVTG SAFEDMLVGV GAKRVRNLFA
KAKKAAPCII FIDEIDSVGS KRGKYEISAG SATDQTLNQL LAEMDGFSTR TGIIVMAATN
RLDVLDDALL RPGRFDRHIQ VNLPDIKERE AILKIHSRNK NISSKVNLLD IARRTPGFSG
AQLENVLNEA TLLAVRADRT SISLTDIDEA IDRVIAGPAK KSRVISDFEK NQVAHHEAGH
ALVGLHLKGA DEVQKITIIP RGQAGGYTLS TPKDAELNLK KKSDLLNMIA GALGGRASEE
LFFGKDAIST GASNDFYKAT NIAKTMVTQL GMSDLGITQF LPSEGGINPN ARYYSENTAQ
RIDEAIAKIL EEQYQVAYNI IKDNQNELKL IVEALLIQET IVKNDIDYIH EHLKLPEAII
KLKEEQLKEK AAAEKEEQAE KAKLDHQSDS AQPQEEPTAS TASSN
