ID   ARTD_METJA              Reviewed;         154 AA.
AC   P81329;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable archaeosortase D {ECO:0000303|PubMed:22037399};
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:D4GUZ4};
GN   Name=artD {ECO:0000303|PubMed:22037399}; OrderedLocusNames=MJ1469.1;
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 D subfamily. {ECO:0000305|PubMed:22037399}.
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DR   EMBL; L77117; AAB99490.1; -; Genomic_DNA.
DR   RefSeq; WP_010870990.1; NC_000909.1.
DR   AlphaFoldDB; P81329; -.
DR   STRING; 243232.MJ_1469.1; -.
DR   TCDB; 9.B.297.3.1; the archaeosortase/exosortase/rhomosortase (sortase) family.
DR   EnsemblBacteria; AAB99490; AAB99490; MJ_1469.1.
DR   GeneID; 1452374; -.
DR   KEGG; mja:MJ_1469.1; -.
DR   eggNOG; arCOG04471; Archaea.
DR   HOGENOM; CLU_1599045_0_0_2; -.
DR   OMA; TCSLEMA; -.
DR   OrthoDB; 124884at2157; -.
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; IPR026432; Archaeo_ArtD.
DR   InterPro; IPR026392; Exo/Archaeosortase_dom.
DR   TIGRFAMs; TIGR04175; archaeo_artD; 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..154
FT                   /note="Probable archaeosortase D"
FT                   /id="PRO_0000107355"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        64
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:D4GUZ4"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D4GUZ4"
SQ   SEQUENCE   154 AA;  18128 MW;  0CC1081E2F38B045 CRC64;
     MGNKNAIYIL RFLIYFFIFY YILKMLEGNI MDLLTITLSK LLNLKFYKNE IIVGKNIIEI
     SSPCTCSLEM ALFLGYIFGT PDVPIKYKIS YSVFGLSIIT ISNILRIILI INYSNMINYN
     VVHDVISFII FPIALFLNWF WIYLLKMKKI IMFK