ID A0A1S6QJF8_9LACO Unreviewed; 700 AA. AC A0A1S6QJF8; DT 10-MAY-2017, integrated into UniProtKB/TrEMBL. DT 10-MAY-2017, sequence version 1. DT 10-APR-2019, entry version 11. 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 Lactobacillus curieae. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. 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 CC metallopeptidase for both cytoplasmic and membrane proteins. Plays CC a role in the quality control of integral membrane proteins. CC {ECO:0000256|HAMAP-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- CC Rule:MF_01458}; CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01458}; Cytoplasmic side {ECO:0000256|HAMAP- CC 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 CC M41 family. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase CC family. {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 STRING; 1138822.PL11_09795; -. DR KEGG; lcu:PL11_007305; -. DR KO; K03798; -. DR OrthoDB; 190468at2; -. DR Proteomes; UP000030361; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:ATPase activity; IEA:UniProtKB-UniRule. 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 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 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; SSF140990; 1. DR SUPFAM; SSF52540; SSF52540; 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}; KW 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030361}; KW Hydrolase {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|HAMAP-Rule:MF_01458}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; KW Protease {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 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT TRANSMEM 134 153 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT DOMAIN 222 361 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 230 237 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}. FT COILED 644 664 {ECO:0000256|SAM:Coils}. FT ACT_SITE 453 453 {ECO:0000256|HAMAP-Rule:MF_01458}. FT METAL 452 452 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 456 456 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 528 528 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT 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 //