FTSH_MYCPN
ID FTSH_MYCPN Reviewed; 709 AA.
AC P75120; Q50345;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=MPN_671;
GN ORFNames=MP171;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 530-585.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x;
RA Proft T., Herrmann R.;
RT "Identification and characterization of hitherto unknown Mycoplasma
RT pneumoniae proteins.";
RL Mol. Microbiol. 13:337-348(1994).
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; U00089; AAB95819.1; -; Genomic_DNA.
DR EMBL; Z32663; CAA83582.1; -; Genomic_DNA.
DR PIR; S73497; S73497.
DR RefSeq; NP_110360.1; NC_000912.1.
DR RefSeq; WP_010875028.1; NC_000912.1.
DR AlphaFoldDB; P75120; -.
DR SMR; P75120; -.
DR STRING; 272634.MPN_671; -.
DR EnsemblBacteria; AAB95819; AAB95819; MPN_671.
DR GeneID; 66608640; -.
DR KEGG; mpn:MPN_671; -.
DR PATRIC; fig|272634.6.peg.737; -.
DR HOGENOM; CLU_000688_16_2_14; -.
DR OMA; QYGMTER; -.
DR BioCyc; MPNE272634:G1GJ3-1074-MON; -.
DR Proteomes; UP000000808; 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; IPR011546; Pept_M41_FtsH_extracell.
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; PF06480; FtsH_ext; 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..709
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084640"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 47..171
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 193..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 673..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 491
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 268..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 494
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 709 AA; 77735 MW; D07585386C8B4C94 CRC64;
MKKNKGLNEA TTSEKPQFPK RTAWKIFWWV VILAIIIGIL VYILMPRATT AVIEKWELSG
TTLSAQIKGL SGKHTFQRIN NSTYVTDDIL QVSISFQGIN PIVVTAHKAT NGSGETIFNI
ANLSINQSTG KAIVNGMMTQ DQKSNNGTEL ASIKGLHDIG TFVAPDTRAR DVLNIFFGLL
PIIIFVIFFL LFWRSARGIS GGGRSEEDNI FSIGKTQAKL AKSSVRFDNI AGLQEEKHEL
LEIVDYLKNP LKYAQMGARS PRGVILYGPP GTGKTLLAKA VAGEAGVPFF QSTGSGFEDM
LVGVGAKRVR DLFNKAKKAA PCIIFIDEID SVGSKRGRVE LSSYSVVEQT LNQLLAEMDG
FTSRTGVVVM AATNRLDVLD DALLRPGRFD RHIQINLPDI KEREGILQVH AKNKNLSSKI
SLLDVAKRTP GFSGAQLENV INEATLLAVR DNRTTINMND IDEAIDRVIA GPAKKSRVVS
DADRKLVAYH EAGHALVGLH VHSNDEVQKI TIIPRGQAGG YTLSTPKSGD LNLKRKSDLL
AMIATAMGGR AAEEEIYGPL EITTGASSDF YKATNIARAM VTQLGMSKLG QVQYVPSQGT
VPPGTKLFSE QTAKDIDFEI NAIIEEQYKK ARTIIKTNRK ELELLVEALL IAETILKSDI
DYIHEHTKLP PEILAQKQEQ QAKQKAEAKE AKLNKKTEKD TEKDSETNS
