ID G0LXY0_APPPP Unreviewed; 599 AA.
AC G0LXY0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458};
GN Name=hflB {ECO:0000313|EMBL:CCA94598.1};
GN Synonyms=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
OS Apple proliferation phytoplasma.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Candidatus Phytoplasma;
OC 16SrX (Apple proliferation group).
OX NCBI_TaxID=37692 {ECO:0000313|EMBL:CCA94598.1};
RN [1] {ECO:0000313|EMBL:CCA94598.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3-8 {ECO:0000313|EMBL:CCA94601.1}, and Rol-1
RC {ECO:0000313|EMBL:CCA94598.1};
RX PubMed=21899439; DOI=10.1094/MPMI-05-11-0126;
RA Seemuller E., Kampmann M., Kiss E., Schneider B.;
RT "HflB gene-based phytopathogenic classification of 'Candidatus phytoplasma
RT mali' strains and evidence that strain composition determines virulence in
RT multiply infected apple trees.";
RL Mol. Plant Microbe Interact. 24:1258-1266(2011).
RN [2] {ECO:0000313|EMBL:CCA94598.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3-8 {ECO:0000313|EMBL:CCA94601.1}, and Rol-1
RC {ECO:0000313|EMBL:CCA94598.1};
RA Schneider B.L.;
RL Submitted (MAY-2011) 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:0000256|HAMAP-
CC Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01458};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01458};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01458};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044, ECO:0000256|HAMAP-
CC Rule:MF_01458}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}.
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DR EMBL; FR863640; CCA94598.1; -; Genomic_DNA.
DR EMBL; FR863643; CCA94601.1; -; Genomic_DNA.
DR AlphaFoldDB; G0LXY0; -.
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 CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 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 NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
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; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW ECO:0000256|RuleBase:RU003651};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01458};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01458};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01458}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 206..345
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT ACT_SITE 437
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 214..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 599 AA; 67658 MW; C71F59903E3BEC58 CRC64;
MKYKKKNILF ITTIIVIYLA FLFNWLEIGI FKPKGESISE SEMLSKISRK DISESVRYSV
YKTMFLKDKP FDIRNVYQIE LTTHNNEKFH AEIIKNTKEE LSFELLPRNK ISYQYEFRPF
SWLLSIFSIL LNFIHVLSSL VFTTYIFLAI HRESGKLNSK SLITSKQKSL FTFKDVAGNT
EEKEEMTELI DFLKQPQKYE TIGAAIPRGV LLEGPPGTGK TLLAKALAGE ANVPFYAVSG
SEFVEMYVGV GASRVRKLFK EAKLNAPCVL FIDEIDVLGG RRGGNSSGGN QEKDQTLNQL
LTEMDGFTPS QGIIVIGATN RADMLDAALL RPGRFDRKIL VNLPDIKSRA EILKLHAQNK
KLSPDINFHQ LAQQTPGMSG AQLAAVLNEA SILTVRNHKD FITMTELSEA LDRVLMGPAK
KSIKYDLEER RMVAYHEAGH AVIGIKLKHA QKVQKITIIP RGNAGGYNLM MPEKETFFSS
RKRMLAQIQS FLGGRVAEEL VFDDISSGAF DDFRQATKIA RLMVTKYGMS DLGVSQDSEF
SDKKLIDTAI KKIIDTCYQQ VQIIIKENKD LLDQIAHLLL EQETITKEEI EKLVVNTKK
//