FTSH_LACPJ
ID FTSH_LACPJ Reviewed; 745 AA.
AC C6VKW6;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=JDM1_0445;
OS Lactiplantibacillus plantarum (strain JDM1) (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=644042;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM1;
RX PubMed=19465650; DOI=10.1128/jb.00587-09;
RA Zhang Z.-Y., Liu C., Zhu Y.-Z., Zhong Y., Zhu Y.-Q., Zheng H.-J.,
RA Zhao G.-P., Wang S.-Y., Guo X.-K.;
RT "Complete genome sequence of Lactobacillus plantarum JDM1.";
RL J. Bacteriol. 191:5020-5021(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 -!- 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; CP001617; ACT61334.1; -; Genomic_DNA.
DR RefSeq; WP_003643854.1; NC_012984.1.
DR AlphaFoldDB; C6VKW6; -.
DR SMR; C6VKW6; -.
DR MEROPS; M41.009; -.
DR PRIDE; C6VKW6; -.
DR GeneID; 57024321; -.
DR GeneID; 66448597; -.
DR KEGG; lpj:JDM1_0445; -.
DR HOGENOM; CLU_000688_16_2_9; -.
DR OMA; QYGMTER; -.
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; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..745
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400347"
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
