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Database: UniProt
Entry: A0A1G1P9R1_9BACT
LinkDB: A0A1G1P9R1_9BACT
Original site: A0A1G1P9R1_9BACT 
ID   A0A1G1P9R1_9BACT        Unreviewed;       273 AA.
AC   A0A1G1P9R1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 13.
DE   RecName: Full=Exosortase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A3C36_05815 {ECO:0000313|EMBL:OGX38593.1};
OS   Omnitrophica WOR_2 bacterium RIFCSPHIGHO2_02_FULL_52_10.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801858 {ECO:0000313|EMBL:OGX38593.1, ECO:0000313|Proteomes:UP000177305};
RN   [1] {ECO:0000313|EMBL:OGX38593.1, ECO:0000313|Proteomes:UP000177305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGX38593.1}.
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DR   EMBL; MHGR01000014; OGX38593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1P9R1; -.
DR   Proteomes; UP000177305; Unassembled WGS sequence.
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   NCBIfam; TIGR02602; 8TM_EpsH; 1.
DR   NCBIfam; TIGR04178; exo_archaeo; 1.
DR   Pfam; PF09721; Exosortase_EpsH; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        40..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        68..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   273 AA;  30734 MW;  D53E5D3E6F8E212C CRC64;
     MKENFIQKNI KPLVAGVFFL IIYIPTQLWM WDRWFAADSY YSHGILIPFV SAYLIWQKRT
     ELAKTQKARS GWGLPLILMG MLAHAFGSLM RVYFISGFSM LLVLVGLILF LYGSQVFKKI
     MFPVLFLAFM IPVPMVLVTS ISFKMKIFAA KIAATVLNNS GIPAVRDGSL IRMRHAQVVV
     DDVCSGLRSL ISLLALGSIF AYWMKSTMGR RLVLFLTAIP IAIITNVMRV VFLSYVAEIW
     GVEIASGVLH DVSGFLVFAL AFVLLYVMVR ILE
//
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