ID W8GEW5_9MOLU Unreviewed; 718 AA.
AC W8GEW5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=ftsH {ECO:0000256|HAMAP-Rule:MF_01458,
GN ECO:0000313|EMBL:AHK22138.1};
GN ORFNames=X271_00015 {ECO:0000313|EMBL:AHK22138.1};
OS Candidatus Hepatoplasma crinochetorum Av.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Hepatoplasma.
OX NCBI_TaxID=1427984 {ECO:0000313|EMBL:AHK22138.1, ECO:0000313|Proteomes:UP000019450};
RN [1] {ECO:0000313|EMBL:AHK22138.1, ECO:0000313|Proteomes:UP000019450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Av {ECO:0000313|EMBL:AHK22138.1,
RC ECO:0000313|Proteomes:UP000019450};
RX PubMed=24482531; DOI=10.1093/gbe/evu020;
RA Leclercq S., Dittmer J., Bouchon D., Cordaux R.;
RT "Phylogenomics of "Candidatus Hepatoplasma crinochetorum," a Lineage of
RT Mollicutes Associated with Noninsect Arthropods.";
RL Genome Biol. Evol. 6:407-415(2014).
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}.
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DR EMBL; CP006932; AHK22138.1; -; Genomic_DNA.
DR AlphaFoldDB; W8GEW5; -.
DR STRING; 1427984.X271_00015; -.
DR KEGG; hcr:X271_00015; -.
DR PATRIC; fig|1427984.3.peg.15; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_14; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000019450; Chromosome.
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 FTSH 2, CHLOROPLASTIC-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000019450};
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 86..106
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 197..219
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 279..417
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 511
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 287..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 514
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 588
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 718 AA; 80414 MW; 28893B018511212C CRC64;
MFLNDSSIKE QDLLSLRGED PNSKNNNSES NSEVEKDKKS NSKENEKNQD NKSKQNTDLN
NPSPKTEKKP VGPIPPKKKK SSLSTILWLL FFFFLILILF ALIFNVNYTY LTPTELADQI
NSAVIGTSID INGLVIQDSD QLVQVTVIID APSGYEYYYT YFANVDDYQT WLEDSILASN
PNILNIDYSL SYQTTSVFWS LVAFLLPLII IVGITVWIFK KIIQSQSNIG KASKKTLLPQ
ISNVRFSDVQ GYEEIKQELY EIVDFLKQPD KYSKFGARTP KGVMLSGPPG TGKTLFAKAI
AGEATIPFYS ISGSDFVEMF VGVGASRVRS LFEQAKKTSP SLIFIDELDA VGRRRGAGPG
GNDEREQTLN QLLVEMDGFS PNSGIIVIAA TNRPDVLDPA LKRPGRFDRL IDIRLPDVKE
REAILRLHGS KGNKKFSKDV NWINISMRTP GFSGAELENV INEAAILAVR EKLNEITLDT
IDEAIDRVIG GPAKANNAMS QEEKILIAHH EAGHALIGLI LKDAERVQKI SIVPRGSAGG
YVLMTPKKEK IIQTKAELNA KIISYLGGRV SEEIFFGKDE ITTGAYSDIQ EATKIARRMI
MDFGMSENLG AIQWNSQEVN SYGMYEKNSV SEKVSELIDK EIRELINKSY VKAHEIISNN
KPMIELFAKA LLIKEILNTE DIDYIYKNKK LTNEMIELEK KENLNSKKTK ENNKTDKK
//
