FTSH_ACIFD
ID FTSH_ACIFD Reviewed; 660 AA.
AC C7M0M0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Afer_1606;
OS Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC 103882 /
OS ICP).
OC Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidimicrobium.
OX NCBI_TaxID=525909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP;
RX PubMed=21304635; DOI=10.4056/sigs.1463;
RA Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Acidimicrobium ferrooxidans type strain
RT (ICP).";
RL Stand. Genomic Sci. 1:38-45(2009).
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; CP001631; ACU54528.1; -; Genomic_DNA.
DR RefSeq; WP_015799007.1; NC_013124.1.
DR AlphaFoldDB; C7M0M0; -.
DR SMR; C7M0M0; -.
DR STRING; 525909.Afer_1606; -.
DR PRIDE; C7M0M0; -.
DR EnsemblBacteria; ACU54528; ACU54528; Afer_1606.
DR KEGG; afo:Afer_1606; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_11; -.
DR OMA; NDGRAWM; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000000771; 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; 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 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..660
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_5000506699"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 46..118
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 140..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 660 AA; 71888 MW; 2931B240CAC8EB74 CRC64;
MMPSSQRPSP RGSRQSPSPD QRGRIAFAIL ATLVVAVLLL TLFSHAPSGQ PLGYSTFIHD
VQAKQVRTAV LNNTTGQITG SLTNGTAYSV TGPLPYTSSE LSTLSKAHVQ VSYITPGPGI
ASTIIEYVIF FGIFIGIWVY LTRRTQGSVN GIMSVGRSRA KTYTTERPKT TFDDVAGYQG
VKGEVKEVVD FLRDPSRFSQ LGARIPKGIL LVGPPGTGKT LLARAVAGEA GVPFMSVSGS
DFMEMFVGVG AARVRDLFQT ARRQSPSIIF IDEIDSIGRK RGTGLGGGHD EREQTLNQML
SEMDGFDPAE GIVVMAATNR PDILDPALLR PGRFDRQIVV PLPDLPERLA ILQVHTRGKR
LAPDVDLEVM AKGTPGMSGA DLANLVNEAA LNAVRRGATD IAMADFDSAR DRIIMGQRRE
ATILSDEEKE RVAFHEGGHA VLAYVLDYSD PVHKVTILPT GMALGVTQQL PERDRHLYPR
EYIEDTLVVR MGGRVAELLV YGDLSTGAAN DLQGNTELAR RMVREWGMSE RLGPMAWGSQ
NVVFLGEDLL HSAEYSDRTA RLVDEEVERI LREQEERATE LLRQHLPGLI AVAHALLERE
TISGEEVGRL VDEAAGHPIH PDGKRVLPIA KLPEYAELEQ FTVTNGNNHA ASHDDTDPVS
