FTSH_RHOM4
ID FTSH_RHOM4 Reviewed; 697 AA.
AC D0MGU8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Rmar_0836;
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Rhodothermus.
OX NCBI_TaxID=518766;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10;
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(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 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 -!- 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; CP001807; ACY47733.1; -; Genomic_DNA.
DR RefSeq; WP_012843345.1; NC_013501.1.
DR AlphaFoldDB; D0MGU8; -.
DR SMR; D0MGU8; -.
DR STRING; 518766.Rmar_0836; -.
DR MEROPS; M41.007; -.
DR EnsemblBacteria; ACY47733; ACY47733; Rmar_0836.
DR KEGG; rmr:Rmar_0836; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_10; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000002221; 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 inner membrane; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..697
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400385"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 51..158
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 180..697
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 475
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 251..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 478
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 697 AA; 78338 MW; 4616785CB1B4B012 CRC64;
MSQNERDSLE LERKNTPPDG PRLPERRPRF SVWIYLAIFL ALLVHFFLFW TGTDTSTIEY
SQFLEYVEKG YVERVEIVND TKVQGRFTEA AVREGLVSVP VRQTDLLRGA QTPELIRRFT
TTKPADHDLT SFLLAYNERA RAEGRPTVQF TARIEENWFG GLLTWIFPLI LIVALWVFLL
RRMSPSSQVL NIGKNRAILY DAMGDHRVTF KDVAGLDEAK EEVAEIVEFL KNPKKFTRLG
GKLPKGVLLV GPPGTGKTLL AKAVAGEAGV PFFSISGSDF VEMFVGVGAA RVRDLFRQAK
EKAPCIIFID EIDAIGRSRG RGIMMGANDE RENTLNQLLV EMDGFNTDKG VIIMAATNRP
DVLDPALLRP GRFDRQILID KPDRRERLEI FKVHTRDLIL GDDVDLEVLA GQTPGFAGAE
IANVCNEAAL LAARKGKEAV EMEDFEQAID RVIAGLEKKN KIISPEEREI VAYHEAGHAI
VGWFLRYTDP VVKVSIVPRG LAALGYAQYL PEERYLYTKE ALLDRMTMAI GGRVAEELVF
GRISTGAQND LERITRMAYA MVVDYGMSER VGYVSFNLSG QYGEQAFFDK PYSEETARLI
DEEVRRIINE VRERARRILE EKRDKLEALA RRLLEKEVLG PRDLVEILGP RPYGDYPSPN
GKDVEELKDL QKGEPTSSSA VEAPAPQTER PESSSAP
