FTSH1_ALKMQ
ID FTSH1_ALKMQ Reviewed; 590 AA.
AC A6TSZ1;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 1 {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH1 {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=Amet_3170;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(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 -!- 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; CP000724; ABR49309.1; -; Genomic_DNA.
DR RefSeq; WP_012064275.1; NC_009633.1.
DR AlphaFoldDB; A6TSZ1; -.
DR SMR; A6TSZ1; -.
DR STRING; 293826.Amet_3170; -.
DR EnsemblBacteria; ABR49309; ABR49309; Amet_3170.
DR KEGG; amt:Amet_3170; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_9; -.
DR OMA; FQQNEGV; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000001572; 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; 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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..590
FT /note="ATP-dependent zinc metalloprotease FtsH 1"
FT /id="PRO_5000256654"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 30..103
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 125..590
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 419
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 195..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 496
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 590 AA; 65095 MW; 3577613707853BEF CRC64;
MLKLTKKQLI IVLGIAIVVV SAIGYAVYTQ YFNEDKLEIS YTAFLESTEA GEIRTVNLSE
GPKLTGVFED GKQFITDHPR TDSLKENLLL HGIQVRETTD QYSVVQVITF VVLIGGFIGV
AIFLSKKNAT QTSKEYDKMS DVEFSTQKDS SIRFADIAGN QEAKENAMEL VDFLKNPEKY
SRYGAKMPKG VILYGSPGTG KTLLARALAS EAGVEFLAVS GSDFVQVYAG LGAGRIRNLF
KKAKDKGKCV IFIDEIDAIG KKRDRGGLGG SDESDRTLNA LLTEMSGFKG SEGIIVMAAT
NRLDILDDAL LRPGRFDRQI EIGLPDLKAR QDILQLYTQN RPIDPKVCLR GIAQQTVYFS
GAKLENLMNE AAIYAAREEA DFITEGHIDK AFYTVVAGEE KKDRSNIQPI DRKITAYHEA
GHAVATKLLC PQNKVTKVTI IPSTKGAGGF SMNIPPDQMY HTKNSMVNSI KVALSGRIIE
EIVFGPDFVT TGASNDIQKA TEILGAMIKQ FGMNDEVGMI NYDVLFGRQG ACDQRVMELT
KLNMKRLYDE TKVLLEKSLN IVEAVAEDLL IKETLKEDEI NEIFSGFQSM
