ID   ARTE_METJA              Reviewed;         184 AA.
AC   Q60336;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Probable archaeosortase E {ECO:0000303|PubMed:22037399};
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:D4GUZ4};
GN   Name=artE {ECO:0000303|PubMed:22037399}; OrderedLocusNames=MJ0027;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   NOMENCLATURE, AND GENE FAMILY.
RX   PubMed=22037399; DOI=10.1128/jb.06026-11;
RA   Haft D.H., Payne S.H., Selengut J.D.;
RT   "Archaeosortases and exosortases are widely distributed systems linking
RT   membrane transit with posttranslational modification.";
RL   J. Bacteriol. 194:36-48(2012).
CC   -!- FUNCTION: Transpeptidase that recognizes and modifies its substrate by
CC       proteolytic cleavage of a sorting signal. Following cleavage, a
CC       covalent intermediate is formed via a thioester bond between the
CC       archaeosortase and its substrate, which is then transferred and
CC       covalently attached to the cell membrane.
CC       {ECO:0000250|UniProtKB:D4GUZ4}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the exosortase/archaeosortase family.
CC       Archaeosortase E subfamily. {ECO:0000305|PubMed:22037399}.
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DR   EMBL; L77117; AAB98013.1; -; Genomic_DNA.
DR   PIR; C64303; C64303.
DR   RefSeq; WP_010869519.1; NC_000909.1.
DR   AlphaFoldDB; Q60336; -.
DR   SMR; Q60336; -.
DR   STRING; 243232.MJ_0027; -.
DR   TCDB; 9.B.297.4.1; the archaeosortase/exosortase/rhomosortase (sortase) family.
DR   EnsemblBacteria; AAB98013; AAB98013; MJ_0027.
DR   GeneID; 1450865; -.
DR   KEGG; mja:MJ_0027; -.
DR   eggNOG; arCOG04471; Archaea.
DR   HOGENOM; CLU_134207_0_0_2; -.
DR   OMA; NGEYIHN; -.
DR   OrthoDB; 105606at2157; -.
DR   Proteomes; UP000000805; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR026485; Archaeo_ArtE.
DR   InterPro; IPR026392; Exo/Archaeosortase_dom.
DR   InterPro; IPR019127; Exosortase.
DR   Pfam; PF09721; Exosortase_EpsH; 1.
DR   TIGRFAMs; TIGR04124; archaeo_artE; 1.
DR   TIGRFAMs; TIGR04178; exo_archaeo; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..184
FT                   /note="Probable archaeosortase E"
FT                   /id="PRO_0000106660"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        90
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:D4GUZ4"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D4GUZ4"
SQ   SEQUENCE   184 AA;  21259 MW;  DA95536BB790C5B4 CRC64;
     MGSLLMERNF MVEDTFTNGK LSKKEKILFL IKFYIIFLVV FFILSYFGKY LIGIVTYLSY
     IFTKIIISDA RLADNFIYLP NNTVEVVEEC TGSFLIAGLL ALIIVYSKNI KEFIIGIFFV
     LLAFFVNIFR IVLICYLVNM HPESSYLYHE IAGYGVILTL VPVLVIGYLK IIEKYRHSSN
     KSHL