FTSH_MYCTU
ID FTSH_MYCTU Reviewed; 760 AA.
AC P9WQN3; L0TD18; P0A4V8; P0C5C0; P96942;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
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=Rv3610c;
GN ORFNames=MTCY07H7B.12;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9729123; DOI=10.1016/s0378-1119(98)00248-0;
RA Anilkumar G., Chauhan M.M., Ajitkumar P.;
RT "Cloning and expression of the gene coding for FtsH protease from
RT Mycobacterium tuberculosis H37Rv.";
RL Gene 214:7-11(1998).
RN [3]
RP CHARACTERIZATION, AND SUBSTRATES.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16684108; DOI=10.1111/j.1574-6968.2006.00251.x;
RA Srinivasan R., Anilkumar G., Rajeswari H., Ajitkumar P.;
RT "Functional characterization of AAA family FtsH protease of Mycobacterium
RT tuberculosis.";
RL FEMS Microbiol. Lett. 259:97-105(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- FUNCTION: Complements an E.coli null mutation. Upon overexpression in
CC E.coli has been shown to degrade endogenous sigma-32, SecY and phage
CC lambda cII protein.
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:0000305|PubMed:9729123};
CC Multi-pass membrane protein {ECO:0000305|PubMed:9729123}; Cytoplasmic
CC side {ECO:0000305|PubMed:9729123}. Note=Upon expression in E.coli.
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; AL123456; CCP46433.1; -; Genomic_DNA.
DR PIR; C70956; C70956.
DR RefSeq; NP_218127.1; NC_000962.3.
DR RefSeq; WP_003419543.1; NZ_NVQJ01000056.1.
DR AlphaFoldDB; P9WQN3; -.
DR SMR; P9WQN3; -.
DR STRING; 83332.Rv3610c; -.
DR MEROPS; M41.015; -.
DR PaxDb; P9WQN3; -.
DR DNASU; 885732; -.
DR GeneID; 885732; -.
DR KEGG; mtu:Rv3610c; -.
DR TubercuList; Rv3610c; -.
DR eggNOG; COG0465; Bacteria.
DR OMA; QYGMTER; -.
DR PhylomeDB; P9WQN3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
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; IBA:GO_Central.
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; IMP:MTBBASE.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MTBBASE.
DR GO; GO:0006979; P:response to oxidative stress; IDA:MTBBASE.
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; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..760
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084644"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 27..110
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 132..760
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 616..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 203..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 760 AA; 81986 MW; AFEF8DBF10E7C6CF CRC64;
MNRKNVTRTI TAIAVVVLLG WSFFYFSDDT RGYKPVDTSV AITQINGDNV KSAQIDDREQ
QLRLILKKGN NETDGSEKVI TKYPTGYAVD LFNALSAKNA KVSTVVNQGS ILGELLVYVL
PLLLLVGLFV MFSRMQGGAR MGFGFGKSRA KQLSKDMPKT TFADVAGVDE AVEELYEIKD
FLQNPSRYQA LGAKIPKGVL LYGPPGTGKT LLARAVAGEA GVPFFTISGS DFVEMFVGVG
ASRVRDLFEQ AKQNSPCIIF VDEIDAVGRQ RGAGLGGGHD EREQTLNQLL VEMDGFGDRA
GVILIAATNR PDILDPALLR PGRFDRQIPV SNPDLAGRRA VLRVHSKGKP MAADADLDGL
AKRTVGMTGA DLANVINEAA LLTARENGTV ITGPALEEAV DRVIGGPRRK GRIISEQEKK
ITAYHEGGHT LAAWAMPDIE PIYKVTILAR GRTGGHAVAV PEEDKGLRTR SEMIAQLVFA
MGGRAAEELV FREPTTGAVS DIEQATKIAR SMVTEFGMSS KLGAVKYGSE HGDPFLGRTM
GTQPDYSHEV AREIDEEVRK LIEAAHTEAW EILTEYRDVL DTLAGELLEK ETLHRPELES
IFADVEKRPR LTMFDDFGGR IPSDKPPIKT PGELAIERGE PWPQPVPEPA FKAAIAQATQ
AAEAARSDAG QTGHGANGSP AGTHRSGDRQ YGSTQPDYGA PAGWHAPGWP PRSSHRPSYS
GEPAPTYPGQ PYPTGQADPG SDESSAEQDD EVSRTKPAHG
