ID A0A1S6QJF8_9LACO Unreviewed; 700 AA. AC A0A1S6QJF8; DT 10-MAY-2017, integrated into UniProtKB/TrEMBL. DT 10-MAY-2017, sequence version 1. DT 22-FEB-2023, entry version 26. 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 ORFNames=PL11_007305 {ECO:0000313|EMBL:AQW21740.1}; OS Lentilactobacillus curieae. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lentilactobacillus. OX NCBI_TaxID=1138822 {ECO:0000313|EMBL:AQW21740.1, ECO:0000313|Proteomes:UP000030361}; RN [1] {ECO:0000313|EMBL:AQW21740.1, ECO:0000313|Proteomes:UP000030361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCTCC M 2011381 {ECO:0000313|EMBL:AQW21740.1, RC ECO:0000313|Proteomes:UP000030361}; RX PubMed=26021929; RA Wang Y., Wang Y., Lang C., Wei D., Xu P., Xie J.; RT "Genome Sequence of Lactobacillus curieae CCTCC M 2011381T, a Novel RT Producer of Gamma-aminobutyric Acid."; RL Genome Announc. 3:0-0(2015). 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 --------------------------------------------------------------------------- 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; CP018906; AQW21740.1; -; Genomic_DNA. DR RefSeq; WP_035168647.1; NZ_CP018906.1. DR AlphaFoldDB; A0A1S6QJF8; -. DR STRING; 1138822.PL11_09795; -. DR EnsemblBacteria; AQW21740; AQW21740; PL11_007305. DR KEGG; lcu:PL11_007305; -. DR eggNOG; COG0465; Bacteria. DR OrthoDB; 9809379at2; -. DR Proteomes; UP000030361; 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:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00009; AAA; 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; 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 TIGRFAMs; TIGR01241; FtsH_fam; 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}; Cell cycle {ECO:0000313|EMBL:AQW21740.1}; KW Cell division {ECO:0000313|EMBL:AQW21740.1}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01458}; KW Membrane {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:UP000030361}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01458}. FT TRANSMEM 12..30 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT TRANSMEM 134..153 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 222..361 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 624..700 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 626..640 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 641..700 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 453 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 230..237 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 452 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 456 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 528 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 700 AA; 76944 MW; A20B431C8BB02F45 CRC64; MNSNKNGLFR SSLFYIVMFL LVMGVIYFFS GSNTNTQSQE IRSSQFVQNL KDDKIKNFSI QPSGGVYKVT GEYRQAQKVK EQTGLLIGGS TQTKDVSKFS TTVLENNTSV AEITKAAQDN KVKMNAKPEE SSGFWVNLLV YVLPLVIFIW FFYMMMGKAG GQGGGNGRVM NFGKSKAKPA DSKQNKVRFS DVAGEEEEKQ ELVEVVEFLK DPRKFTSLGA KIPHGVLLEG PPGTGKTLLA KAVAGEAGVP FYSISGSDFV EMFVGVGASR VRDLFEQAKK AAPAIIFIDE IDAVGRKRGA GMGGGHDERE QTLNQLLVEM DGFEGNEGVI VIAATNRSDV LDPALTRPGR FDRKILVGRP DVNGREAILK VHSKNKPLSS NVDLHEIAKQ TPGFVGADLA NLLNEAALLA ARRNKADIDA SDVDEAEDRV IAGPAKRNRV ISKHERETVA YHEAGHTIVG LVLNDARVVH KVTIVPRGRA GGYAIMLPKE DQQLMSKKDA QEQIAGLMGG RAAEEIIFNS ESSGASNDFE QATNIARAMV TQYGMSDKLG RVQLENPSEE AYGPRYSQET AASIDDEVRR FTDEGHAEAT RIIEEHRDQH RIIAEALLKY ETLDEKQILS LYNTGKMPED PSTSDFPSER ASTFEEAKRE LERKEAERQA SIEKGKDNSD ETDTSSTDPQ PDDVKPDNDS QNNHQNNDDE //