ID   EPSH_METS1              Reviewed;         304 AA.
AC   Q83VR1;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Probable exosortase EpsH {ECO:0000305};
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:D4GUZ4};
GN   Name=epsH {ECO:0000303|PubMed:12624205};
OS   Methylobacillus sp. (strain 12S).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus; unclassified Methylobacillus.
OX   NCBI_TaxID=94001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=12S;
RX   PubMed=12624205; DOI=10.1099/mic.0.25913-0;
RA   Yoshida T., Ayabe Y., Yasunaga M., Usami Y., Habe H., Nojiri H., Omori T.;
RT   "Genes involved in the synthesis of the exopolysaccharide methanolan by the
RT   obligate methylotroph Methylobacillus sp strain 12S.";
RL   Microbiology 149:431-444(2003).
RN   [2]
RP   PREDICTED FUNCTION.
RX   PubMed=16930487; DOI=10.1186/1741-7007-4-29;
RA   Haft D.H., Paulsen I.T., Ward N., Selengut J.D.;
RT   "Exopolysaccharide-associated protein sorting in environmental organisms:
RT   the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling
RT   heuristic.";
RL   BMC Biol. 4:29-29(2006).
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       exosortase and its substrate, which is then transferred and covalently
CC       attached to the cell membrane (By similarity). This sortase may
CC       recognize a tripartite structure consisting of a conserved Pro-Glu-Pro
CC       (PEP) 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). {ECO:0000250|UniProtKB:D4GUZ4,
CC       ECO:0000305|PubMed:16930487}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene does not significantly
CC       alter exopolysaccharide (EPS) production.
CC       {ECO:0000269|PubMed:12624205}.
CC   -!- SIMILARITY: Belongs to the exosortase/archaeosortase family. Exosortase
CC       EpsH subfamily. {ECO:0000305}.
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DR   EMBL; AB062506; BAC55138.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q83VR1; -.
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; IPR013426; EpsH-like.
DR   InterPro; IPR026392; Exo/Archaeosortase_dom.
DR   InterPro; IPR019127; Exosortase.
DR   InterPro; IPR017544; Exosortase-2.
DR   Pfam; PF09721; Exosortase_EpsH; 1.
DR   TIGRFAMs; TIGR02602; 8TM_EpsH; 1.
DR   TIGRFAMs; TIGR04178; exo_archaeo; 1.
DR   TIGRFAMs; TIGR03113; exosortase_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..304
FT                   /note="Probable exosortase EpsH"
FT                   /id="PRO_0000444297"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        195
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:D4GUZ4"
FT   ACT_SITE        241
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D4GUZ4"
SQ   SEQUENCE   304 AA;  34406 MW;  F3EBAD5105C08C04 CRC64;
     MEKHIKHAIR WPSLDTIPWA WVAIAIGLLI LYFPTFWDLF HGLWGTERHA HGPIVFFVSI
     WFFYFKFKQL PEYGITYDPS PKLGWPILVL GLLLFILGRS QTLLIFEVGS LIPVLLGITL
     IFMGTRVAKF LWFAFFFLCF VVPLPAFVVD AATLPMKTAV SFATAHILYA LDYPIARTGV
     MLTIGQYQLL VADACAGLNS LFTLEVLGLL YMNVTHHESP FRNFMLAVLI IPISFIANVT
     RVIVLALITY HWGDAAGQGF LHEFSGIVLF ITALMLVIAT DSLLRFFSRK FEKVPSTQSV
     DLKR