(data stored in ACNUC1104 zone)

SWISSPROT: D3UYY4_XENBS

ID   D3UYY4_XENBS            Unreviewed;       638 AA.
AC   D3UYY4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458};
DE            EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458};
GN   Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458,
GN   ECO:0000313|EMBL:CBJ79512.1};
GN   OrderedLocusNames=XBJ1_0362 {ECO:0000313|EMBL:CBJ79512.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79512.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79512.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79512.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Acts as a processive, ATP-dependent zinc
CC       metallopeptidase for both cytoplasmic and membrane proteins. Plays
CC       a role in the quality control of integral membrane proteins.
CC       {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01458};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01458};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01458}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_01458}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase
CC       M41 family. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01458}.
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DR   EMBL; FN667741; CBJ79512.1; -; Genomic_DNA.
DR   RefSeq; WP_012986971.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0362; -.
DR   MEROPS; M41.001; -.
DR   EnsemblBacteria; CBJ79512; CBJ79512; XBJ1_0362.
DR   GeneID; 8829986; -.
DR   KEGG; xbo:XBJ1_0362; -.
DR   PATRIC; fig|406818.4.peg.332; -.
DR   eggNOG; ENOG4105C3H; Bacteria.
DR   eggNOG; COG0465; LUCA.
DR   HOGENOM; HOG000217276; -.
DR   KO; K03798; -.
DR   OMA; MNKRWRN; -.
DR   BioCyc; XBOV406818:XBJ1_RS01580-MONOMER; -.
DR   Proteomes; UP000002045; 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; D3UYY4.
DR   SWISS-2DPAGE; D3UYY4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:CBJ79512.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:CBJ79512.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   TRANSMEM      7     25       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   TRANSMEM    102    123       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   DOMAIN      188    327       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     196    203       ATP. {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   ACT_SITE    419    419       {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   METAL       418    418       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       422    422       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       496    496       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
SQ   SEQUENCE   638 AA;  70229 MW;  8C97DB2A3D0B52F4 CRC64;
     MSDMAKNLIL WLVIAVVLMV LFQSFGPGDS SGRRVDYSNF ISELSQNQVR EVRISGRDID
     YSKKDDGKKY STYMPIQDEK LLDTLLNKQV KVIGEPPEQQ GLLATLFISW FPMLLLIGVW
     IFFMRQMQGG GGKGAMSFGK SKARMLTEDQ IKTTFADVAG CDEAKEEVGE LVEYLREPGR
     FQKLGGKIPK GILMVGPPGT GKTLLAKAIA GEAKVPFFTI SGSDFVEMFV GVGASRVRDM
     FEQAKKSAPC IIFIDEIDAV GRQRGAGLGG GHDEREQTLN QMLVEMDGFE GNEGIIVIAA
     TNRPDVLDPA LLRPGRFDRQ VVVGLPDVRG REQILKVHMR RIPLDTDVDA SIIARGTPGF
     SGADLANLAN EAALFAARGN KRVVSMVEFE KAKDKIMMGA ERRSMVMTEE QKESTAYHEA
     GHAIIGRLVP EHDPVHKVTI IPRGRALGVT FFLPEGDQIS ASRQKLESQL STLYGGRLAE
     EIIYGVDSVS TGASNDIKVA TSIARNMVTQ WGFSEKLGPL LYAEEEGEIF LGRSVAKAKH
     MSEDTARLID QEVKAIVDRN YQRARKILMD NLDILHSMKD ALMKYETIDV SQIDDLMNRT
     TVRSPAGWEG DNNNGGNNRH NMSSPQQTVK PADGNPTA
//

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