FTSH_LACPL
ID FTSH_LACPL Reviewed; 745 AA.
AC Q88Z31; F9UL20;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
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}; OrderedLocusNames=lp_0547;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
RN [3]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=19074391; DOI=10.1128/jb.01551-08;
RA Fiocco D., Collins M., Muscariello L., Hols P., Kleerebezem M., Msadek T.,
RA Spano G.;
RT "The Lactobacillus plantarum ftsH gene is a novel member of the CtsR stress
RT response regulon.";
RL J. Bacteriol. 191:1688-1694(2009).
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 -!- INDUCTION: Expressed at a low constitutive level, expression is
CC increased after exposure to 42 degrees Celsius. Transcription is
CC partially repressed by CtsR. {ECO:0000269|PubMed:19074391}.
CC -!- DISRUPTION PHENOTYPE: Cells grow more slowly under optimal conditions,
CC and much mre slowly at 42 degrees Celsius.
CC {ECO:0000269|PubMed:19074391}.
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; AY644764; AAU05734.1; -; Genomic_DNA.
DR EMBL; AL935263; CCC78035.1; -; Genomic_DNA.
DR RefSeq; WP_003643854.1; NC_004567.2.
DR RefSeq; YP_004888549.1; NC_004567.2.
DR AlphaFoldDB; Q88Z31; -.
DR SMR; Q88Z31; -.
DR STRING; 220668.lp_0547; -.
DR MEROPS; M41.009; -.
DR EnsemblBacteria; CCC78035; CCC78035; lp_0547.
DR GeneID; 57024321; -.
DR GeneID; 66448597; -.
DR KEGG; lpl:lp_0547; -.
DR PATRIC; fig|220668.9.peg.453; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_9; -.
DR OMA; QYGMTER; -.
DR PhylomeDB; Q88Z31; -.
DR BioCyc; LPLA220668:G1GW0-456-MON; -.
DR Proteomes; UP000000432; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Protease; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..745
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400346"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 33..131
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 153..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 630..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 450
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 227..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 745 AA; 80803 MW; 0690A8E2D72D74F6 CRC64;
MNNRRNGLFR NSLFYILMFL SLMGIIYFFF GGNSGSQTQN IRYSEFVKQL DKNNVKNVSI
QPSGGVYKVT GSYRKARTTS SANALGIKSA STKTTSFSTT MLENNSTVDQ VSKLAAKHDV
KVTAKAEESS GIWVTLLMYI APVILMLFLF YMMMGQAGQG GGNNRVMNFG KTKAKPADSK
QNKVRFSDVA GEEEEKQELV EVVEFLKDPR KFVSLGARIP SGVLLEGPPG TGKTLLAKAV
AGEAGVPFFS ISGSDFVEMF VGVGASRVRD LFEQAKKNAP SIIFIDEIDA VGRQRGNGMG
GGHDEREQTL NQLLVEMDGF TGNEGVIVMA ATNRSDVLDP ALLRPGRFDR KILVGRPDVK
GREAILKVHA KNKPLAADVD LKEIAKQTPG FVGADLENLL NEAALLAARR NKKQVDAADL
DEAEDRVIAG PAKHDRVVNK HERETVAYHE AGHTIVGLVL NDARVVHKVT IVPRGRAGGY
AIMLPREDQM LMSKRDAKEQ MAGLMGGRAA EEIIFGAQSS GASNDFEQAT QIARAMVTQY
GMSEKLGPVE LENANQQAAY QQGMGASAFS QHTAQLIDDE VRRLSQEAHQ TATDIIESHR
EQHKLIAEAL LKYETLDEKQ ILSLFKTGKM PEKDSNEFPS EKAATFEESK RELERREAEK
HAQNQSADDK QADSADTTTN VSVAEPSFPS ESDASSEVSA DSSVNSTANS ATESATDSDV
ATSATGLPNA ESATPSSQDD TNSQA
