ARTA_HALVD
ID ARTA_HALVD Reviewed; 303 AA.
AC D4GUZ4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Archaeosortase A {ECO:0000303|PubMed:22037399};
DE EC=3.4.22.- {ECO:0000269|PubMed:23651326, ECO:0000269|PubMed:26712937, ECO:0000269|PubMed:29465796};
GN Name=artA {ECO:0000303|PubMed:22037399}; Synonyms=cyo;
GN OrderedLocusNames=HVO_0915; ORFNames=C498_14173;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70;
RX PubMed=23651326; DOI=10.1111/mmi.12248;
RA Abdul Halim M.F., Pfeiffer F., Zou J., Frisch A., Haft D., Wu S., Tolic N.,
RA Brewer H., Payne S.H., Pasa-Tolic L., Pohlschroder M.;
RT "Haloferax volcanii archaeosortase is required for motility, mating, and C-
RT terminal processing of the S-layer glycoprotein.";
RL Mol. Microbiol. 88:1164-1175(2013).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26712937; DOI=10.1128/jb.00849-15;
RA Abdul Halim M.F., Karch K.R., Zhou Y., Haft D.H., Garcia B.A.,
RA Pohlschroder M.;
RT "Permuting the PGF signature motif blocks both archaeosortase-dependent C-
RT terminal cleavage and prenyl lipid attachment for the Haloferax volcanii S-
RT layer glycoprotein.";
RL J. Bacteriol. 198:808-815(2015).
RN [6]
RP FUNCTION.
RC STRAIN=H53;
RX PubMed=28069824; DOI=10.1128/jb.00802-16;
RA Abdul Halim M.F., Stoltzfus J.D., Schulze S., Hippler M., Pohlschroder M.;
RT "ArtA-dependent processing of a Tat substrate containing a conserved
RT tripartite structure that is not localized at the C terminus.";
RL J. Bacteriol. 199:E00802-E00802(2017).
RN [7]
RP CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-173; ARG-214 AND
RP ARG-253.
RX PubMed=29465796; DOI=10.1111/mmi.13935;
RA Abdul Halim M.F., Rodriguez R., Stoltzfus J.D., Duggin I.G.,
RA Pohlschroder M.;
RT "Conserved residues are critical for Haloferax volcanii archaeosortase
RT catalytic activity: implications for convergent evolution of the catalytic
RT mechanisms of non-homologous sortases from archaea and bacteria.";
RL Mol. Microbiol. 108:276-287(2018).
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 (Probable). This sortase
CC recognizes a tripartite structure consisting of a conserved Pro-Gly-Phe
CC (PGF) motif, followed by a transmembrane alpha helix domain and a
CC cluster of basic residues, usually at the C-terminus of target proteins
CC (Probable). Confirmed substrates include the cell surface S-layer
CC glycoprotein Csg and HVO_0405 (PubMed:23651326, PubMed:26712937,
CC PubMed:28069824). ArtA is required for the C-terminal processing of Csg
CC and for its lipidation and attachment to the archaeal plasma membrane
CC (PubMed:23651326, PubMed:26712937). It is also required for the
CC processing of HVO_0405, which contains an atypical central tripartite
CC structure (PubMed:28069824). {ECO:0000269|PubMed:23651326,
CC ECO:0000269|PubMed:26712937, ECO:0000269|PubMed:28069824,
CC ECO:0000305|PubMed:23651326, ECO:0000305|PubMed:26712937}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene results in poor growth,
CC especially under low-salt conditions, alterations in cell shape and in
CC the S-layer, impaired motility and impaired conjugation.
CC {ECO:0000269|PubMed:23651326}.
CC -!- SIMILARITY: Belongs to the exosortase/archaeosortase family.
CC Archaeosortase A subfamily. {ECO:0000305|PubMed:22037399}.
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DR EMBL; CP001956; ADE02650.1; -; Genomic_DNA.
DR EMBL; AOHU01000096; ELY26918.1; -; Genomic_DNA.
DR RefSeq; WP_004044024.1; NZ_AOHU01000096.1.
DR AlphaFoldDB; D4GUZ4; -.
DR STRING; 309800.C498_14173; -.
DR TCDB; 9.B.297.1.1; the archaeosortase/exosortase/rhomosortase (sortase) family.
DR EnsemblBacteria; ADE02650; ADE02650; HVO_0915.
DR EnsemblBacteria; ELY26918; ELY26918; C498_14173.
DR GeneID; 8926366; -.
DR KEGG; hvo:HVO_0915; -.
DR PATRIC; fig|309800.29.peg.2725; -.
DR eggNOG; arCOG04471; Archaea.
DR HOGENOM; CLU_065734_1_0_2; -.
DR OMA; IYLPFET; -.
DR OrthoDB; 100786at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..303
FT /note="Archaeosortase A"
FT /id="PRO_0000428764"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 173
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305|PubMed:29465796"
FT ACT_SITE 214
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:29465796"
FT SITE 253
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:29465796"
FT MUTAGEN 173
FT /note="C->A,S: Lack of processing activity."
FT /evidence="ECO:0000269|PubMed:29465796"
FT MUTAGEN 214
FT /note="R->A: Lack of processing activity."
FT /evidence="ECO:0000269|PubMed:29465796"
FT MUTAGEN 253
FT /note="R->A: Retains some processing activity but does not
FT complement deletion mutant."
FT /evidence="ECO:0000269|PubMed:29465796"
SQ SEQUENCE 303 AA; 33092 MW; EF7CBD37E473E8BF CRC64;
MPGLLSDILA WVVIGTFVAG AVANGRDREL GRRVMTAAWV LFALFWLQLI PHFTLVHKSY
IEGLLTIAAV PASLYAGWLL YNGRDTLFVL SRAVAAMGVV YLPFETIPAF TLLGATVPAP
RGVLMETVAA QTRFLIESLG YTPQMIVGDQ GYLNTFLWMQ GSHRLEISVV LACTGLGSIA
IFAGLIAAVD APMGRKLRGL AIAVPIIYAL NLLRTTFIAI SVGKQYFHLF VDEVLFLFGS
SDPYMVSFFI SDRIISQALA VVALVGVTYL VVHEVPELLT VIEDVLYMVT GDEYDLRNEL
GLD
