(data stored in SCRATCH3701 zone)

SWISSPROT: FTSH_RICTY

ID   FTSH_RICTY              Reviewed;         637 AA.
AC   Q68XR9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 96.
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=RT0087;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
DR   EMBL; AE017197; AAU03573.1; -; Genomic_DNA.
DR   RefSeq; WP_011190560.1; NC_006142.1.
DR   SMR; Q68XR9; -.
DR   STRING; 257363.RT0087; -.
DR   MEROPS; M41.001; -.
DR   PRIDE; Q68XR9; -.
DR   EnsemblBacteria; AAU03573; AAU03573; RT0087.
DR   KEGG; rty:RT0087; -.
DR   eggNOG; ENOG4105C3H; Bacteria.
DR   eggNOG; COG0465; LUCA.
DR   HOGENOM; HOG000217277; -.
DR   KO; K03798; -.
DR   OMA; DRQIYVD; -.
DR   OrthoDB; 190468at2; -.
DR   BioCyc; RTYP257363:G1G0L-90-MONOMER; -.
DR   Proteomes; UP000000604; 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:ATPase activity; IEA:UniProtKB-UniRule.
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   Gene3D; 1.20.58.760; -; 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;
DR   PRODOM; Q68XR9.
DR   SWISS-2DPAGE; Q68XR9.
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..637
FT                   /note="ATP-dependent zinc metalloprotease FtsH"
FT                   /id="PRO_0000272337"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        28..103
FT                   /note="Periplasmic"
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..637
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   NP_BIND         195..202
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   ACT_SITE        418
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   METAL           417
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   METAL           421
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   METAL           495
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   637 AA;  69979 MW;  8EF54EB66B97BBBB CRC64;
     MNNQGRSILA WAALFIFVIL LFNVFQSDGL LGVRNNITFS DFLTRVDERT INSVKIQGRV
     IEGTSNDGST FSTYSPDYPD LVNRLTSNDV NIEVVPLETR MNTFLGFLIS WFPMLLLIGV
     WVFFMRQMHG GGKAMGFGKS KARLLSDKGP KITFKDVAGI DEAKEELTEI VDFLRDPSKF
     QKLGGKIPKG CLLIGPPGTG KTLLAKAIAG EANVPFFSIS GSDFVEMFVG VGASRVRDMF
     EQGKRNAPCI IFIDEIDAVG RHRGIGMGGG NDEREQTLNQ MLVEMDGFEA NEGVVIIAAT
     NRPDVLDRAL LRPGRFDRQI AVANPDINGR EQILKVHLKK IKYNSTVLAR IIARGTPGFS
     GAELANLVNE AALIAARLGK KEVDMHDMEE AKDKVLMGVV RRSIAMSEKE KRLTAYHEGG
     HALVGLYCPA ASPIHKATII PRGNALGMVQ RLPETDEYSQ NREQMESSIA VYMAGRVAEE
     IIFGKNKVTS GAASDIKGAT NIARAMVTKA GLSDLIGPIF HGSSSDDMYG RQQSNEISEA
     TAKLIDAEVK KIITQGYEFA KDILTKHIDQ LHTLANALIE YETLSGQQIK NLLSGRALDS
     EEENKFPFND AHTIKIDKEK LHEKTKTTKA QKENIAS
//

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