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FTSH_STRM9
ID   FTSH_STRM9              Reviewed;         683 AA.
AC   D1AXT4;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Smon_0632;
OS   Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 /
OS   9901).
OC   Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Streptobacillus.
OX   NCBI_TaxID=519441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14647 / DSM 12112 / NCTC 10651 / 9901;
RX   DOI=10.4056/sigs.48727;
RA   Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S.,
RA   Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D.,
RA   Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C., Pati A.,
RA   Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Rohde M., Sproer C., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptobacillus moniliformis type strain
RT   (9901T).";
RL   Stand. Genomic Sci. 1:300-307(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; CP001779; ACZ01110.1; -; Genomic_DNA.
DR   RefSeq; WP_012858662.1; NC_013515.1.
DR   AlphaFoldDB; D1AXT4; -.
DR   SMR; D1AXT4; -.
DR   STRING; 519441.Smon_0632; -.
DR   EnsemblBacteria; ACZ01110; ACZ01110; Smon_0632.
DR   GeneID; 29673784; -.
DR   KEGG; smf:Smon_0632; -.
DR   eggNOG; COG0465; Bacteria.
DR   HOGENOM; CLU_000688_16_2_0; -.
DR   OMA; QYGMTER; -.
DR   OrthoDB; 190468at2; -.
DR   Proteomes; UP000002072; 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 inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW   Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..683
FT                   /note="ATP-dependent zinc metalloprotease FtsH"
FT                   /id="PRO_0000400399"
FT   TOPO_DOM        1..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        92..174
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        196..683
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        495
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         270..277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
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         498
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   683 AA;  76269 MW;  BE72AC869CEA6634 CRC64;
     MEDKNIKDDE ILDDQNDNQE DVQNQDEEKE IKPKKPKKKV YISDDENAEE IKKRIESLKN
     KNNNISFRVK PPIFFFLILI LMSTLFYFYG NKTALFQEKR EISYTQFVTK VKQGDITEIR
     ESQEKLTGIK KVAGKVEVFE TNKLTDRLGQ DTYLMEISKE KNVNIVVLGT PVSSIITRAI
     FSFAPLFMLL FFFYFINKKM MGSSGGVIGN PFNIGKGKGK ISERPNVKFS DVAGLTEEKE
     ELKEIVEFLK NPARFEKAGA RVPKGVLLLG EPGTGKTLLA KAVAGESEAA FFPISGSEFI
     ELYVGVGASR VRELFKDAKK EAPAIIFIDE IDAVGRRRGQ NKNGGGGNEE REQTLNQLLV
     EMDGFDTDQR IIVMAATNRS DVLDPALLRG GRFDRRIEVS RPDVKGRIEI LKVHSRNKKL
     ASDVKLEDIA KITPGFVGAD LENLLNEAAI LAARKNSDEI TMEDLDEAVD KVGMGLGQKS
     KIISKRDKDM LAYHEGGHAL AATLIPGANK VHKVTIIPRG DAGGYMMPLP EETLGKTRKQ
     ILAEINVLFA GRAGEELMMD DIATGAYSDI KRATELAKLL ISSVGMSELG PINYEHSDNG
     FMLSSDLSNE TAREIDLEVR KLLKFKYEET LNLLRDNKET LEKIATLLKE KETVTGSEIR
     ALVSGSSVNE VLELDDEQLE KYY
 
 
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