FTSH_BACSU
ID FTSH_BACSU Reviewed; 637 AA.
AC P37476;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 154.
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};
DE AltName: Full=Cell division protease FtsH;
GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=BSU00690;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION.
RC STRAIN=1012;
RX PubMed=7608085; DOI=10.1128/jb.177.14.4105-4112.1995;
RA Deuerling E., Paeslack B., Schumann W.;
RT "The ftsH gene of Bacillus subtilis is transiently induced after osmotic
RT and temperature upshift.";
RL J. Bacteriol. 177:4105-4112(1995).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=1012;
RX PubMed=9076729; DOI=10.1046/j.1365-2958.1997.2721636.x;
RA Deuerling E., Mogk A., Richter C., Purucker M., Schumann W.;
RT "The ftsH gene of Bacillus subtilis is involved in major cellular processes
RT such as sporulation, stress adaptation and secretion.";
RL Mol. Microbiol. 23:921-933(1997).
RN [5]
RP SPOIVFA AS A POSSIBLE SUBSTRATE.
RX PubMed=10464210; DOI=10.1128/jb.181.17.5384-5388.1999;
RA Resnekov O.;
RT "Role of the sporulation protein BofA in regulating activation of the
RT Bacillus subtilis developmental transcription factor sigmaK.";
RL J. Bacteriol. 181:5384-5388(1999).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10851010; DOI=10.1128/jb.182.13.3870-3873.2000;
RA Wehrl W., Niederweis M., Schumann W.;
RT "The FtsH protein accumulates at the septum of Bacillus subtilis during
RT cell division and sporulation.";
RL J. Bacteriol. 182:3870-3873(2000).
RN [7]
RP ATPASE AND PROTEASE ACTIVITIES, AND MUTAGENESIS OF LYS-207 AND GLU-424.
RC STRAIN=1012;
RX PubMed=15386101; DOI=10.1007/s00284-004-4319-2;
RA Kotschwar M., Harfst E., Ohanjan T., Schumann W.;
RT "Construction and analyses of mutant ftsH alleles of Bacillus subtilis
RT involving the ATPase- and Zn-binding domains.";
RL Curr. Microbiol. 49:180-185(2004).
RN [8]
RP SPO0E AS SUBSTRATE, AND DEVELOPMENTAL STAGE.
RC STRAIN=1012;
RX PubMed=19332814; DOI=10.1099/mic.0.024182-0;
RA Le A.T., Schumann W.;
RT "The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH
RT metalloprotease.";
RL Microbiology 155:1122-1132(2009).
RN [9]
RP INTERACTION WITH FLOA AND FLOT, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [10]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
RN [11]
RP EZRA AS A POSSIBLE SUBSTRATE, AND STABILIZATION BY FLOA AND FLOT.
RC STRAIN=168 / PY79;
RX PubMed=24222488; DOI=10.1128/mbio.00719-13;
RA Mielich-Suess B., Schneider J., Lopez D.;
RT "Overproduction of flotillin influences cell differentiation and shape in
RT Bacillus subtilis.";
RL MBio 4:0-0(2013).
RN [12]
RP INTERACTION WITH FLOT.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=26297017; DOI=10.1099/mic.0.000137;
RA Schneider J., Mielich-Suess B., Boehme R., Lopez D.;
RT "In vivo characterization of the scaffold activity of flotillin on the
RT membrane kinase KinC of Bacillus subtilis.";
RL Microbiology 161:1871-1887(2015).
RN [13]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=27362352; DOI=10.1371/journal.pgen.1006116;
RA Dempwolff F., Schmidt F.K., Hervas A.B., Stroh A., Roesch T.C., Riese C.N.,
RA Dersch S., Heimerl T., Lucena D., Huelsbusch N., Stuermer C.A.,
RA Takeshita N., Fischer R., Eckhardt B., Graumann P.L.;
RT "Super Resolution Fluorescence Microscopy and Tracking of Bacterial
RT Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein
RT Microdomains within the Bacterial Membrane but Absence of Clusters
RT Containing Detergent-Resistant Proteins.";
RL PLoS Genet. 12:e1006116-e1006116(2016).
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: In vitro partially degrades Spo0E, the phosphatase that acts
CC on Spo0A-P. Recognition requires the last 14 residues of Spo0E
CC (PubMed:19332814). Its stabile accumulation requires FlotA and Flot
CC (PubMed:24222488). May degrade EzrA (Probable).
CC {ECO:0000269|PubMed:19332814, ECO:0000269|PubMed:24222488,
CC ECO:0000305|PubMed:24222488}.
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 (By similarity). Interacts with FloT at midcell
CC (Probable) (PubMed:23651456, PubMed:26297017). Interacts with FloA at
CC midcell (Probable). Another study shows only minor colocalization with
CC FloA or FloT (PubMed:27362352). {ECO:0000255|HAMAP-Rule:MF_01458,
CC ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:26297017,
CC ECO:0000269|PubMed:27362352, ECO:0000305|PubMed:22882210}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:27362352,
CC ECO:0000305|PubMed:10851010}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:10851010}; Cytoplasmic side
CC {ECO:0000305|PubMed:10851010}. Membrane raft
CC {ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456,
CC ECO:0000269|PubMed:27362352}; Multi-pass membrane protein.
CC Note=Accumulates in the midcell septum during vegetative cell division.
CC At the septa colocalizes with FloA and FloT, which seem to stabilize it
CC in the membrane (PubMed:10851010, PubMed:22882210). At the onset of
CC sporulation appears at positions near the cell poles that may coincide
CC with future division sites. Then, FtsH becomes concentrated at the
CC sporulation septum and disappears from the distal pole
CC (PubMed:10851010). Present in detergent-resistant membrane (DRM)
CC fractions that may be equivalent to eukaryotic membrane rafts; these
CC rafts include proteins involved in signaling, molecule trafficking and
CC protein secretion (PubMed:22882210, PubMed:23651456).
CC {ECO:0000269|PubMed:10851010, ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:23651456}.
CC -!- DEVELOPMENTAL STAGE: Necessary only for stage 0 of sporulation.
CC {ECO:0000269|PubMed:19332814}.
CC -!- INDUCTION: Induced by osmotic shock (0.8 M NaCl) and by heat shock (52
CC degrees Celsius). {ECO:0000269|PubMed:7608085}.
CC -!- DISRUPTION PHENOTYPE: Required for expression of the stage 0
CC sporulation gene Spo0A, as well as for a normal heat or osmotic stress
CC response, cells lacking this gene grow as long filaments and tend to
CC lyse upon entry into stationary phase. Secretion of some extracellular
CC proteins is also reduced (PubMed:9076729). Loss of biofilm formation
CC (PubMed:22882210). {ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:9076729}.
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; D26185; BAA05304.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11845.1; -; Genomic_DNA.
DR PIR; E69627; E69627.
DR RefSeq; NP_387950.1; NC_000964.3.
DR RefSeq; WP_003243881.1; NZ_JNCM01000028.1.
DR AlphaFoldDB; P37476; -.
DR SMR; P37476; -.
DR IntAct; P37476; 8.
DR MINT; P37476; -.
DR STRING; 224308.BSU00690; -.
DR MEROPS; M41.009; -.
DR jPOST; P37476; -.
DR PaxDb; P37476; -.
DR PRIDE; P37476; -.
DR EnsemblBacteria; CAB11845; CAB11845; BSU_00690.
DR GeneID; 938094; -.
DR KEGG; bsu:BSU00690; -.
DR PATRIC; fig|224308.179.peg.69; -.
DR eggNOG; COG0465; Bacteria.
DR InParanoid; P37476; -.
DR OMA; QYGMTER; -.
DR PhylomeDB; P37476; -.
DR BioCyc; BSUB:BSU00690-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0030428; C:cell septum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030163; P:protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0043934; P:sporulation; IMP:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW Reference proteome; Stress response; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..637
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084627"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 29..109
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 131..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 514..637
FT /note="Not necessary for FtsH function"
FT ACT_SITE 424
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 201..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT MUTAGEN 207
FT /note="K->N: Does not complement an ftsH deletion, loss of
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:15386101"
FT MUTAGEN 424
FT /note="E->Q: Does not complement an ftsH deletion, loss of
FT protease activity against casein."
FT /evidence="ECO:0000269|PubMed:15386101"
SQ SEQUENCE 637 AA; 70937 MW; C62B6C518B91C9D3 CRC64;
MNRVFRNTIF YLLILLVVIG VVSYFQTSNP KTENMSYSTF IKNLDDGKVD SVSVQPVRGV
YEVKGQLKNY DKDQYFLTHV PEGKGADQIF NALKKTDVKV EPAQETSGWV TFLTTIIPFV
IIFILFFFLL NQAQGGGSRV MNFGKSKAKL YTEEKKRVKF KDVAGADEEK QELVEVVEFL
KDPRKFAELG ARIPKGVLLV GPPGTGKTLL AKACAGEAGV PFFSISGSDF VEMFVGVGAS
RVRDLFENAK KNAPCLIFID EIDAVGRQRG AGLGGGHDER EQTLNQLLVE MDGFSANEGI
IIIAATNRAD ILDPALLRPG RFDRQITVDR PDVIGREAVL KVHARNKPLD ETVNLKSIAM
RTPGFSGADL ENLLNEAALV AARQNKKKID ARDIDEATDR VIAGPAKKSR VISKKERNIV
AYHEGGHTVI GLVLDEADMV HKVTIVPRGQ AGGYAVMLPR EDRYFQTKPE LLDKIVGLLG
GRVAEEIIFG EVSTGAHNDF QRATNIARRM VTEFGMSEKL GPLQFGQSQG GQVFLGRDFN
NEQNYSDQIA YEIDQEIQRI IKECYERAKQ ILTENRDKLE LIAQTLLKVE TLDAEQIKHL
IDHGTLPERN FSDDEKNDDV KVNILTKTEE KKDDTKE
