ID FTSH_CAUVN Reviewed; 626 AA.
AC B8H444;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=CCNA_03334;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11972783; DOI=10.1046/j.1365-2958.2002.02887.x;
RA Fischer B., Rummel G., Aldridge P., Jenal U.;
RT "The FtsH protease is involved in development, stress response and heat
RT shock control in Caulobacter crescentus.";
RL Mol. Microbiol. 44:461-478(2002).
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: Absence of FtsH leads to increased sigma-32 levels, which
CC suggests, in analogy to E.coli, that sigma-32 is a substrate for FtsH.
CC May play a role in the general stress response, as overexpression leads
CC to improved resistance to salt stress.
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- INDUCTION: By heat shock at 40 degrees Celsius.
CC {ECO:0000269|PubMed:11972783}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow more slowly than
CC wild-type, are filamentous and under high-phosphate defective in stalk
CC biogenesis. They are hypersensitive to a range of antibiotics. Cells do
CC not grow at 37 degrees Celsius, or in 50 mM NaCl. Required for
CC stationary phase survival. Depletion leads to increased levels of
CC sigma-32. {ECO:0000269|PubMed:11972783}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001340; ACL96798.1; -; Genomic_DNA.
DR RefSeq; WP_010921059.1; NC_011916.1.
DR RefSeq; YP_002518706.1; NC_011916.1.
DR AlphaFoldDB; B8H444; -.
DR SMR; B8H444; -.
DR MEROPS; M41.001; -.
DR GeneID; 7330358; -.
DR KEGG; ccs:CCNA_03334; -.
DR PATRIC; fig|565050.3.peg.3249; -.
DR HOGENOM; CLU_000688_16_0_5; -.
DR OrthoDB; 9809379at2; -.
DR PhylomeDB; B8H444; -.
DR Proteomes; UP000001364; Chromosome.
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: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; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.720.210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 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 NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
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; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Nucleotide-binding;
KW Protease; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..626
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400335"
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..98
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 120..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 414
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 491
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 626 AA; 67693 MW; 440B3F0956446474 CRC64;
MNFRNLAIWL VIVAVLGGVF VVSQNSRTKS SSEISYSQLL KDVDAGKIKS AEIAGQTVLA
KTADNKTLTV NAPMNSEELV NRMVAKNADV KFKSGSISFL AILVQLLPIL LVVGVWLFLM
RQMQGGAKGA MGFGKSKARL LTENKNRITF EDVAGVDEAK EELQEVVDFL KDPAKFQRLG
GKIPKGALLV GPPGTGKTLI ARAVAGEAGV PFFTISGSDF VEMFVGVGAS RVRDMFEQAK
KNAPCIIFID EIDAVGRHRG AGLGGGNDER EQTLNQLLVE MDGFEANEGI ILIAATNRPD
VLDPALLRPG RFDRQVVVPN PDVAGREKII RVHMKNVPLA ADVDVKTLAR GTPGFSGADL
ANLVNEAALM AARKNRRMVT MQDFEQAKDK VMMGAERRSM AMNEEEKKLT AYHEGGHAIV
ALNVPLADPV HKATIVPRGR ALGMVMQLPE GDRYSMKYQQ MTSRLAIMMG GRVAEEIIFG
KENITSGASS DIKAATDLAR NMVTRWGYSD ILGTVAYGDN QDEVFLGHSV ARTQNVSEET
ARLIDSEVKR LVQYGLDEAR RILTDKIDDL HTLGKALLEY ETLSGEEIAD ILKGIPPKRE
EEEAATAVIA PSLVPLSPGA GASVTA
//
