ID D2RLK1_ACIFV Unreviewed; 645 AA. AC D2RLK1; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 04-NOV-2026, entry version 88. 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 OrderedLocusNames=Acfer_1596 {ECO:0000313|EMBL:ADB47953.1}; OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP OS 106432 / VR4). OC Bacteria; Bacillati; Bacillota; Negativicutes; Acidaminococcales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB47953.1, ECO:0000313|Proteomes:UP000001902}; RN [1] {ECO:0000313|EMBL:ADB47953.1, ECO:0000313|Proteomes:UP000001902} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4 RC {ECO:0000313|Proteomes:UP000001902}; RX PubMed=21304687; DOI=10.4056/sigs.1002553; RA Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C., RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K., RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M., RA Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Acidaminococcus fermentans type strain RT (VR4)."; RL Stand. Genomic Sci. 3:1-14(2010). 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; Evidence={ECO:0000256|HAMAP- CC 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}. Membrane CC {ECO:0000256|ARBA:ARBA00004370}. 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|ARBA:ARBA00061570, ECO:0000256|HAMAP-Rule:MF_01458}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001859; ADB47953.1; -; Genomic_DNA. DR RefSeq; WP_012938937.1; NC_013740.1. DR STRING; 591001.Acfer_1596; -. DR MEROPS; M41.009; -. DR GeneID; 78335287; -. DR KEGG; afn:Acfer_1596; -. DR eggNOG; COG0465; Bacteria. DR HOGENOM; CLU_000688_16_2_9; -. DR OMA; AAFQFFM; -. DR OrthoDB; 9809379at2; -. DR CDD; cd19501; RecA-like_FtsH; 1. DR FunFam; 1.10.8.60:FF:000001; ATP-dependent zinc metalloprotease FtsH; 1. DR FunFam; 1.20.58.760:FF:000001; ATP-dependent zinc metalloprotease FtsH; 1. DR FunFam; 3.40.50.300:FF:000001; ATP-dependent zinc metalloprotease FtsH; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.30.720.210; -; 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; IPR011546; Pept_M41_FtsH_extracell. DR InterPro; IPR000642; Peptidase_M41. DR InterPro; IPR037219; Peptidase_M41-like. 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; PF06480; FtsH_ext; 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 NCBIfam; TIGR01241; FtsH_fam; 1. DR PROSITE; PS00674; AAA; 1. 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:InterPro. DR Proteomes; UP000001902; Chromosome. DR AlphaFoldDB; D2RLK1; -. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01458}; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01458}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP- KW Rule:MF_01458}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01458}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458}; KW Reference proteome {ECO:0000313|Proteomes:UP000001902}; 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..25 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT TRANSMEM 101..122 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 186..325 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 602..645 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 602..614 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 624..639 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 417 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 194..201 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 416 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 420 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 492 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 645 AA; 70856 MW; 2FFBF5D69CE98CAF CRC64; MSKFIRNLVF YLLIVIVGVW IYDYYNASST PKNEMSYSNF VKEVQQDEVK SVTIVDNSVI KGKLKNGAEF TTIAPRDEKL VDTLRARDVE IRAELPPQPS MLSNILTSLL PMVVIVILWF FMMNNAQGGG SRVMSFGKSK AKLYGDGKSR VTFKDVAGAD EAKQELEEVV EFLKAPQKYN QLGAKIPKGV LLYGPPGTGK TLLAKAVAGE AGVPFFSISG SDFVEMFVGV GASRVRDLFD QAKKNAPCIV FIDEIDAVGR QRGAGLGGGH DEREQTLNQL LVEMDGFGAN EGIIMIAATN RPDILDPALL RPGRFDRQIV VDKPDIRGRR SILRVHTKGK PMDPSVDLGV IARQTPGFTG ADLANLVNEG ALLAARHNQV TITMSDLEEA AERVMMGPER KSRVITDEEK RLTAYHEGGH TLVGMLLDHT DPVHKVTIIP RGRAGGYTLS LPTEDRYYAT RSEMLDQLKV LLGGRVAEAL VLHEISSGAS SDLQRATELA RRMTCEYGMS DVLGAVTFGH RQEQVFLGRD IGRQNDYSEK VAAQIDGEIR RFIDEAYEGT VKLLTDNMDK LHLIAKNLME RETLEGHEIE ELLKYGHILE KGEVPPQEEP EKPADGTPAP VGPLPAEEPA EAPVMAPVPK EVPEG //