FTSH4_SPHTD
ID FTSH4_SPHTD Reviewed; 658 AA.
AC D1C8C0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 4 {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsh4; OrderedLocusNames=Sthe_2649;
OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC Bacteria; Chloroflexi; Sphaerobacteridae; Sphaerobacterales;
OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX NCBI_TaxID=479434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49802 / DSM 20745 / S 6022;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R.,
RA Goeker M., Klenk H.P., Eisen J.A.;
RT "The complete chromosome 2 of Sphaerobacter thermophilus DSM 20745.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001824; ACZ40063.1; -; Genomic_DNA.
DR RefSeq; WP_012873101.1; NC_013524.1.
DR AlphaFoldDB; D1C8C0; -.
DR SMR; D1C8C0; -.
DR STRING; 479434.Sthe_2649; -.
DR EnsemblBacteria; ACZ40063; ACZ40063; Sthe_2649.
DR KEGG; sti:Sthe_2649; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_0; -.
DR OMA; YDKQGGG; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000002027; Chromosome 2.
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..658
FT /note="ATP-dependent zinc metalloprotease FtsH 4"
FT /id="PRO_0000400397"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 50..149
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 171..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 465
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 243..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 468
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"
SQ SEQUENCE 658 AA; 71751 MW; E4289052327BA41C CRC64;
MREPTNRQGS PGPGEPRPPA QGRPRFPTWI LWVALLALAL WNVYTFFWPS SGARLNIPYS
AFIQQVEGEN VSSVTIRGQR VSGTFTEEVR VAGDQVLSPG DPVPPGTSPN EIRTGTQFQT
TIPENSQTEL VPLLQSHGVT VKIDQAGGSV WPSLLATIVP LFLFIGLMVY LGRSMSRGQQ
NVFSFGRSKA RVYDAERPRV TFADVAGEEE AKAELSEVVD FLRNPMKYHA IGARLPRGIL
LVGPPGTGKT LLARAVAGEA GVPFFSVSAS EFVEMFVGVG ASRVRDLFER AKASAPSIMF
VDELDAVGRQ RFAGLGGGND EREQTLNQLL VEMDGFEPHQ DVIVIAATNR PDVLDPALLR
PGRFDRQVTV GLPDRRGREA ILRIHTRGIP VADDLDLEEL AAATPGFSGA DLANLVNEAA
LMAARKNKKI VERIDFDEAL DKIVLGTERA MIMSEHDKRV VAYHEAGHAV AAHFSPGTDP
LRKVSIVPRG QSLGVTIQAP EEDRFNYSRA YLLARLTVMM GGRAAEKLVF NEMTTGAQND
LKEATLLARR MVGLWGMSDE VGPVYLGMGE QHVFLGREIM QDRDVAEATL ERADEAVQRL
LREAMERAEQ LLRKYRDKLD ALAEALIAEE TIGQEKITEI LGAPPVPSAA PAAAADSV
