FTSH_BRAFD
ID FTSH_BRAFD Reviewed; 704 AA.
AC C7MC16;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=Bfae_12800;
OS Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG
OS 19847 / NBRC 14762 / NCIMB 9860 / 6-10).
OC Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae; Brachybacterium.
OX NCBI_TaxID=446465;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 / NCIMB
RC 9860 / 6-10;
RX PubMed=21304631; DOI=10.4056/sigs.492;
RA Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachybacterium faecium type strain
RT (Schefferle 6-10).";
RL Stand. Genomic Sci. 1:3-11(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; CP001643; ACU85123.1; -; Genomic_DNA.
DR RefSeq; WP_012804894.1; NC_013172.1.
DR RefSeq; YP_003154713.1; NC_013172.1.
DR AlphaFoldDB; C7MC16; -.
DR SMR; C7MC16; -.
DR STRING; 446465.Bfae_12800; -.
DR EnsemblBacteria; ACU85123; ACU85123; Bfae_12800.
DR KEGG; bfa:Bfae_12800; -.
DR PATRIC; fig|446465.5.peg.1280; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_1_11; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000001919; 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..704
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400332"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 39..127
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 149..704
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 624..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 440
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 217..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 704 AA; 75758 MW; 308E8DDF92F6BB7B CRC64;
MADSAKTPRG KKRRPFTGLA LWIIVALLLG MAMFSLFGRD GYQQIDTQQG LELLAGDTVE
QAKIIDGNQQ RVDLVLTEDF KDGDEDKGTQ VRFSYVDARG DAVVQAVEDA APAKGYTDEI
ASSSWWSTLL LSFLPLLIFI GLFWFLIMNA QGGGKAMQFG KSKAKLFNKE APKVTFADVA
GADEAVEELD EIKQFLVDPG RYQAVGAKIP KGVLLYGPPG TGKTLLAKAV AGEANVPFYS
ISGSDFVEMF VGVGASRVRD LFNTAKENAP AIIFIDEIDA VGRHRGAGMG GGHDEREQTL
NQMLVEMDGF EENQNVILIA ATNRVDILDP ALLRPGRFDR QIGVEAPDLK GRLHILGVHA
KGKPLAHDVD LEAVAKRAIG MSGADLANVL NEAALLTARS GNQIIDNRAL DEAIDRVSMG
PQRYSKVMTE RERQMTAYHE GGHALVAAAM NNSAPVTKVT ILPRGRAGGY TMVVPTQDRN
YQSRNELLDR LAYAMGGYAV EESIFHDVTT GPSSDLQNAT KIARTMVMQL GMSGTVGQVA
LSGEQDEVFV GMQQGQAPRF SAETASLVDQ EVRTLLDNAL DEAWSVIVEN RHVLDRLVEE
LLEKETLNER ELAQIFRDVK KQPPREVWIS STERPSLAAP SVGGTTTATG TESHDAGEPL
QPNPPELPHP GGEGPQIPGA PHGGEPGGGG YGYDGSAGTD GTGR
