ID D7CIR3_SYNLT Unreviewed; 600 AA. AC D7CIR3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-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=Slip_0128 {ECO:0000313|EMBL:ADI00928.1}; OS Syntrophothermus lipocalidus (strain DSM 12680 / TGB-C1). OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; OC Syntrophomonadaceae; Syntrophothermus. OX NCBI_TaxID=643648 {ECO:0000313|EMBL:ADI00928.1, ECO:0000313|Proteomes:UP000000378}; RN [1] {ECO:0000313|Proteomes:UP000000378} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378}; RX DOI=10.4056/sigs.1233249; RG US DOE Joint Genome Institute (JGI-PGF); RA Djao O., Zhang X., Lucas S., Lapidus A., Glavina Del Rio T., Nolan M., RA Tice H., Cheng J., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., RA Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., RA Jeffries C., Rohde M., Sikorski J., Spring S., Goker M., Detter J., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., RA Klenk H.; RT "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB- RT C1T)."; RL Stand. Genomic Sci. 3:267-275(2010). RN [2] {ECO:0000313|EMBL:ADI00928.1, ECO:0000313|Proteomes:UP000000378} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378}; RX PubMed=21304731; RA Djao O.D., Zhang X., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H., RA Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., RA Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Rohde M., Sikorski J., Spring S., Goker M., Detter J.C., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB- RT C1)."; RL Stand. Genomic Sci. 3:268-275(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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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; CP002048; ADI00928.1; -; Genomic_DNA. DR RefSeq; WP_013174332.1; NC_014220.1. DR AlphaFoldDB; D7CIR3; -. DR STRING; 643648.Slip_0128; -. DR MEROPS; M41.021; -. DR KEGG; slp:Slip_0128; -. DR eggNOG; COG0465; Bacteria. DR HOGENOM; CLU_000688_16_2_9; -. DR OMA; AAHPMEI; -. DR Proteomes; UP000000378; 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:InterPro. 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 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; 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 PROSITE; PS00674; AAA; 1. 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:UP000000378}; KW Signal {ECO:0000256|SAM:SignalP}; 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 SIGNAL 1..26 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 27..600 FT /note="ATP-dependent zinc metalloprotease FtsH" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5054766112" FT TRANSMEM 104..125 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 189..328 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT ACT_SITE 420 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 197..204 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 419 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 423 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 495 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 600 AA; 66553 MW; 5BB03355020F79F0 CRC64; MDRVLKNFAI YAVIVLLAVF AIKATSESEK PTQDVDYSTF YRDVAQDKID QVMITVDTDV YIIEGKYKDG KTFRTEAPKE DNIFEHLRAH NVAYDTEKAK GPPWWTGLLS TLLPIAILVG FIFLMMNQTQ GGGNRVMQFG RSRARMTTPE EVKVTFKDVA GADEAKEELQ EVIEFLKNPQ KFIQMGAKIP KGVLLYGPPG TGKTLMARAV AGEAGVPFFS ISGSDFVEMF VGVGAARVRD LFENAKKNAP CIVFIDEIDA VGRQRGAGVG GGHDEREQTL NQLLVEMDGF STNEGIIVMA GTNRPDILDP ALLRPGRFDR HIVIDRPDVK GREAILKVHA EGKPLAPGVD MSVIAKRTPG FTGADLANVM NEAALLSARR NKKEITMEEL EDAIERVIAG PEKKSRVISE KEKRLVAYHE AGHAVVSYFL PNTDKVHKIS IIPRGRAGGY TLLLPEEDIN YVTKSRLLDE VTTLLGGRVA ESLVLQEVST GAQNDLERAT SIVRRMITEY GMSEELGPLT FGHKREEVFL GRDIARDRNY SEAIAYAIDQ EARGFIENCY EKAKDILTQN IDKLHKVAEK LMEKEVLEGD EFEAIMTGRA //