FTSH3_PHYMT
ID FTSH3_PHYMT Reviewed; 599 AA.
AC B3R0R7;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 3 {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH3 {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=ATP_00464;
OS Phytoplasma mali (strain AT).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; 16SrX (Apple proliferation group).
OX NCBI_TaxID=482235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT;
RX PubMed=18582369; DOI=10.1186/1471-2164-9-306;
RA Kube M., Schneider B., Kuhl H., Dandekar T., Heitmann K., Migdoll A.M.,
RA Reinhardt R., Seemueller E.;
RT "The linear chromosome of the plant-pathogenic mycoplasma 'Candidatus
RT Phytoplasma mali'.";
RL BMC Genomics 9:306-306(2008).
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; CU469464; CAP18651.1; -; Genomic_DNA.
DR AlphaFoldDB; B3R0R7; -.
DR SMR; B3R0R7; -.
DR STRING; 37692.ATP_00464; -.
DR EnsemblBacteria; CAP18651; CAP18651; ATP_00464.
DR KEGG; pml:ATP_00464; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_14; -.
DR OMA; RRSNGMP; -.
DR Proteomes; UP000002020; 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; 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; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..599
FT /note="ATP-dependent zinc metalloprotease FtsH 3"
FT /id="PRO_0000400374"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 29..128
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 150..599
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 437
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 214..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 599 AA; 67535 MW; D9C6952B362AC486 CRC64;
MKYKKKNILF ITTIIVIYLA FLFNWLEIGI FKPKGESISE SEMLSKISRK DISESVRYSV
YKTMFLKDKP FDIRNVYQIE LTTHNNEKFH AEIIKNTKEE LSFELLPRNK ISYQYEFRPF
SWLLSIFSIL LNFINVLSSL VFTIYIFLAI HRESGKLNSK SLITSKQKSL FTFKDVAGNT
EEKEEMTELI DFLKQPQKYE TIGAAIPRGV LLEGPPGTGK TLLAKALAGE ASVPFYAVSG
SEFVEMYVGV GASRVRKLFK EAKLNAPCVL FIDEIDVLGG RRGGNSSGGN QEKDQTLNQL
LTEMDGFTPS QGIIVIGATN RADMLDAALL RPGRFDRKIL VNLPDIKSRA EILKLHAQNK
KLSSDIDFHQ LAQQTPGMSG AQLAAVLNEA SILTVRNHKD FITMTELSEA LDRVLMGPAK
KSIKYDPEER RMVAYHEAGH AVIGIKLKHA QKVQKITIIP RGNAGGYNLM MPEKETFFSS
RKRMLAQIQS FLGGRVAEEL VFDDISSGAF DDFRQATKIA RLMVTKYGMS DLGVSQDSEF
SDKKLIDTAI KKIIDNCYAR TKHLMLENKT LLDQIAHLLL EQETITQAEI EQLVVNTKK
