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Database: UniProt
Entry: G0LXY0_APPPP
LinkDB: G0LXY0_APPPP
Original site: G0LXY0_APPPP 
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
//
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