FTSH_LEUMM
ID FTSH_LEUMM Reviewed; 700 AA.
AC Q03Z46;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=LEUM_0404;
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000414; ABJ61526.1; -; Genomic_DNA.
DR RefSeq; WP_011679262.1; NC_008531.1.
DR AlphaFoldDB; Q03Z46; -.
DR SMR; Q03Z46; -.
DR STRING; 203120.LEUM_0404; -.
DR PRIDE; Q03Z46; -.
DR EnsemblBacteria; ABJ61526; ABJ61526; LEUM_0404.
DR GeneID; 61177116; -.
DR KEGG; lme:LEUM_0404; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_9; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000000362; 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; 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.
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..700
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400350"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 32..130
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 152..700
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 644..700
FT /note="Disordered"
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 700 AA; 76011 MW; 3CF450073B37A17A CRC64;
MNNNKGGFLR SSVFYIFIFL AVVGMVYGLF GNDKTTTKTI TSSEFIKALN DKELKSVTVQ
PGNSIYNVTG TYKKAQTATK DKGLSLFQPT QKVTKFTSTL LPNDASLKSV TDAATKTKTE
LVTKQAENSG FWLNLLVSLV PVLLIVAVFY LMMNQAGGGK GGQGGMMSFG KSKAKPSDPK
DNKVRFADVA GAEEEKQELV EVVEFLKAPK KFVNLGARIP KGVLLEGPPG TGKTLLAKAV
AGEASVPFFS MSGSDFVEMF VGVGASRVRD LFENAKKSAP AIIFIDEIDA VGRRRGTGMG
GGNDEREQTL NQILIEMDGF EGSEGVIILA STNRSDVLDP ALLRSGRFDR KILVGAPDVK
GREAILNVHA KNKPLADNVD LKAIAQQTPG YVGADLENLL NEAALLAARR NKSKVDAADI
DEAEDRIFQG PAKTNHNMSE SERRTTAYHE AGHALVGLVR SEASVVRKVT IVPRGRIGGY
ALMTPKNDRY NLKYSEAKEQ LAGLMGGRAS EIFMFNEASS GASNDFQQAT GLARQMVTAF
GMSDKLGMVQ LEGNASVGYA DQAGNRAYSE ETARLIDEEV RRLAREAFDD AIAILRDNKD
KLTAIAEALL EVETLDEKQI KDIYLTGTFT RKDIQDDTEL AKAKSFEEAK AAADAKDSQA
EQRFEKQDEE KSSDDHSESK NEDTDSTDKS ETDDNNTENK
