ID   ARTA_NATPD              Reviewed;         315 AA.
AC   Q3IS61;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Archaeosortase A {ECO:0000303|PubMed:22037399};
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:D4GUZ4};
GN   Name=artA {ECO:0000303|PubMed:22037399}; OrderedLocusNames=NP_1872A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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 A subfamily. {ECO:0000305|PubMed:22037399}.
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DR   EMBL; CR936257; CAI49027.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3IS61; -.
DR   STRING; 348780.NP_1872A; -.
DR   EnsemblBacteria; CAI49027; CAI49027; NP_1872A.
DR   KEGG; nph:NP_1872A; -.
DR   eggNOG; arCOG04471; Archaea.
DR   HOGENOM; CLU_065734_1_0_2; -.
DR   OMA; IYLPFET; -.
DR   Proteomes; UP000002698; 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; IPR014522; ArtA.
DR   InterPro; IPR026392; Exo/Archaeosortase_dom.
DR   InterPro; IPR019127; Exosortase.
DR   Pfam; PF09721; Exosortase_EpsH; 1.
DR   PIRSF; PIRSF025737; Cyco1; 1.
DR   TIGRFAMs; TIGR04178; exo_archaeo; 1.
DR   TIGRFAMs; TIGR04125; exosort_PGF_TRM; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..315
FT                   /note="Archaeosortase A"
FT                   /id="PRO_0000428765"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        177
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:D4GUZ4"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D4GUZ4"
FT   SITE            259
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:D4GUZ4"
SQ   SEQUENCE   315 AA;  34581 MW;  F2127C8F3806F78A CRC64;
     MSLLEAIAEL HVIPYTDVLA WVVMAAFIAG VAADYRDNLL AARRLTAGAW WLFAVFWFVL
     IQHFAFVHRS VVQTVLILIA VPACLYVGWL VFAGRDSLLT LSRAVAFMTV IYLPFETSEL
     ARGLLIEAVA FQTATVIDAL SLADGMEYMQ DPDEGSTLMN TFWFPETGRA SRVVFECTGI
     GAMSIFGGLI AAVNAPLRRK AVGIALSISI IWVLNIGRNV FIALANGYQW FAYSWLEGPI
     MALFGLTDPA RVSFFVADRV LAQLLAVVAL AGLAWFIARW VPELLDIAEE LLSIVGIDVE
     LHHPSVDRTD TDPAD