FTSH_LACLA
ID FTSH_LACLA Reviewed; 695 AA.
AC P46469;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; Synonyms=tma;
GN OrderedLocusNames=LL0021; ORFNames=L0204;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CHCC285;
RX PubMed=8000529; DOI=10.1099/00221287-140-10-2601;
RA Nilsson D., Lauridsen A.A., Tomoyasu T., Ogura T.;
RT "A Lactococcus lactis gene encodes a membrane protein with putative ATPase
RT activity that is homologous to the essential Escherichia coli ftsH gene
RT product.";
RL Microbiology 140:2601-2610(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103.
RX PubMed=1465108; DOI=10.1007/bf00279381;
RA Nilsson D., Lauridsen A.A.;
RT "Isolation of purine auxotrophic mutants of Lactococcus lactis and
RT characterization of the gene hpt encoding hypoxanthine guanine
RT phosphoribosyltransferase.";
RL Mol. Gen. Genet. 235:359-364(1992).
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:0000255|HAMAP-
CC Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01458};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01458};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000255|HAMAP-Rule:MF_01458}.
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DR EMBL; X69123; CAA48877.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK04119.1; -; Genomic_DNA.
DR EMBL; X67015; CAA47405.1; -; Genomic_DNA.
DR PIR; E86627; E86627.
DR PIR; S28533; S28533.
DR RefSeq; NP_266177.1; NC_002662.1.
DR RefSeq; WP_003132177.1; NC_002662.1.
DR AlphaFoldDB; P46469; -.
DR SMR; P46469; -.
DR STRING; 272623.L0204; -.
DR MEROPS; M41.009; -.
DR PaxDb; P46469; -.
DR PRIDE; P46469; -.
DR EnsemblBacteria; AAK04119; AAK04119; L0204.
DR GeneID; 60355709; -.
DR GeneID; 66441012; -.
DR KEGG; lla:L0204; -.
DR PATRIC; fig|272623.7.peg.23; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_9; -.
DR OMA; QYGMTER; -.
DR Proteomes; UP000002196; 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: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 Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..695
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084638"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 37..139
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 161..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 657..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 457
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 695 AA; 75561 MW; 1B8A23A4D0307259 CRC64;
MNNNKQPKQG NFVKNILMWV ILAIVVVVGF NFFFSSNQSS VDKISYSQLM TKLDGNKIEN
VTMQPSDSLI TVTGEYKEPV KVKGTNNFPL LGNSSSEVKN FQAYIIPTDS VVKDIQNAAK
SNDVKLSVVQ ASSSGMWVQI LSYIIPMLLF VGIFWLMMGG MGARGGGGGG NPMSFGKSRA
KQQDGKTSKV RFADVAGSEE EKQELVEVVD FLKNPKKYHD LGARIPAGVL LEGPPGTGKT
LLAKAVAGEA GVPFYSISGS DFVEMFVGVG ASRVRDLFEN AKKTAPSIIF IDEIDAVGRQ
RGAGLGGGND EREQTLNQLL VEMDGFQDDG NSVIVIAATN RSDVLDPALL RPGRFDRKVL
VGAPDVKGRE AVLKVHAKNK PLASDVDLHN VATQTPGYVG ADLENVLNEA ALVAARQNKK
EINAADIDEG MDRAMAGPAK KDRIQSMRER EIVAYHEAGH AIVGLVLENG STVRKVTVVP
RGRIGGYMLA LPDEEIMQPT NFHLQDQLAS LMGGRLGEEI VFGVATPGAS NDIEKATHIA
RSMVTEYGMS KKLGMVSYEG DHQVFIGRDY GQTKTYSEAT AVMIDDEVRR ILGEAYDRAK
EAIETHREQH KAIAEALLKY ETLDAKQIMS LFKTGKMPDE AAAAEVPEPK TFEESLKDAN
ANVDDFSNIN IYNGDEKTDS KPEENKEKSE DETAE
