FTSH_RHOE4
ID FTSH_RHOE4 Reviewed; 854 AA.
AC C0ZPK5;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=RER_06250;
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=234621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008957; BAH31333.1; -; Genomic_DNA.
DR RefSeq; WP_020906072.1; NC_012490.1.
DR AlphaFoldDB; C0ZPK5; -.
DR SMR; C0ZPK5; -.
DR STRING; 234621.RER_06250; -.
DR MEROPS; M41.015; -.
DR EnsemblBacteria; BAH31333; BAH31333; RER_06250.
DR KEGG; rer:RER_06250; -.
DR PATRIC; fig|234621.6.peg.1071; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_1_11; -.
DR OMA; QYGMTER; -.
DR Proteomes; UP000002204; 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; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..854
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400382"
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..112
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 134..854
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 658..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 430
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 854 AA; 92150 MW; 8BA653D8B8B794E3 CRC64;
MNRKTVFRNV LLVAVVLLVI YAFSYFSNDT RDFKTVDTSV AISQLDAKNV ASAQIDDREQ
QVRLWLKNGN DATDGKTQIL AKYPASASEQ IFDKVEGAGA DKFNTTVTQE SWLTSILLFV
LPMIILFGIF FFVMNRMQGG GGRGGVMGFG KSKAKQLTKD MPKTTFADVA GADEAVEELY
EIKDFLQNPA RYQALGAKIP RGVLLYGPPG TGKTLLARAV AGEAGVPFFT ISGSDFVEMF
VGVGASRVRD MFEQAKQNSP CIIFVDEIDA VGRQRGAGLG GGHDEREQTL NQLLVEMDGF
GDRTGIILIA ATNRPDILDP ALLRPGRFDR QIPVGAPDLA GRRAILRVHS QGKPIDPNAD
LEGLAKRTVG MSGADLANVI NEAALLTARE NGTVITEASL EESVDRVVGG PRRKSRIISE
HEKKITAYHE GGHTLAAWAM PDIEPVYKVT ILARGRTGGH AMTVPEDDKG LMTRSEMIAR
LVMAMGGRAA EELVFHEPTT GASSDIDMAT KIARAMVTEY GMSAKLGAVR YGQEGGDPFL
GRSMGVQSDY SHEIAREIDE EVRNLIEAAH TEAWAILNEY RDALDLIATE LLERETLTRK
DLEKILAGVE KRPRITAFND FGGRTPSDRP PVKTPRELAI ERGETWPEPA AAPVLVKAGA
PNSGVPNGGV PNNGGLPNNG NQGPSNGYAQ PSYPQPSAPQ QTPQPGTPDY GAPAGWSAPG
WPPRENPSPT YPGQQSGGYT GGQNPTPPNQ SQGQYGQPQH GQPQPDQGQY GQPHPGQQAY
PEQPHPGRRY PAQPDYPVQY PDGGPFADPN RGNPSGENQW QSPTPEQPQT PPPHHSAEDD
GPSTARWDGP DGSR
