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Database: UniProt
Entry: A0A0W0VM86_9GAMM
LinkDB: A0A0W0VM86_9GAMM
Original site: A0A0W0VM86_9GAMM 
ID   A0A0W0VM86_9GAMM        Unreviewed;       271 AA.
AC   A0A0W0VM86;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Methylamine utilization protein MauE {ECO:0000256|ARBA:ARBA00019078};
GN   Name=grxC {ECO:0000313|EMBL:KTD21180.1};
GN   ORFNames=Llon_1278 {ECO:0000313|EMBL:KTD21180.1};
OS   Legionella londiniensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45068 {ECO:0000313|EMBL:KTD21180.1, ECO:0000313|Proteomes:UP000054997};
RN   [1] {ECO:0000313|EMBL:KTD21180.1, ECO:0000313|Proteomes:UP000054997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49505 {ECO:0000313|EMBL:KTD21180.1,
RC   ECO:0000313|Proteomes:UP000054997};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be specifically involved in the processing, transport,
CC       and/or maturation of the MADH beta-subunit.
CC       {ECO:0000256|ARBA:ARBA00003475}.
CC   -!- PATHWAY: One-carbon metabolism; methylamine degradation.
CC       {ECO:0000256|ARBA:ARBA00004856}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {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:KTD21180.1}.
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DR   EMBL; LNYK01000016; KTD21180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0VM86; -.
DR   STRING; 45068.Llon_1278; -.
DR   PATRIC; fig|45068.5.peg.1383; -.
DR   Proteomes; UP000054997; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR045057; Gcn5-rel_NAT.
DR   InterPro; IPR031165; GNAT_YJDJ.
DR   InterPro; IPR009908; Methylamine_util_MauE.
DR   PANTHER; PTHR31435; PROTEIN NATD1; 1.
DR   PANTHER; PTHR31435:SF9; PROTEIN NATD1; 1.
DR   Pfam; PF14542; Acetyltransf_CG; 1.
DR   Pfam; PF07291; MauE; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51729; GNAT_YJDJ; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054997};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        115..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        247..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..100
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51729"
SQ   SEQUENCE   271 AA;  31072 MW;  4BA55FC2E15EDDB2 CRC64;
     MIHYRGQKMD LNIKHDEKNQ RFYATKNDEE SELKYKKIDD TTLDYFTTFV PEGLRHQGIA
     AEITKHALEY AKENGYKIVP TCPFVKNFID EHPKYQNLVK KKSEKSSDES SLKRYWPLLS
     LIIVSFLAAL SINWQVGGDM RVWMHYFMGI FLVIFSTLKL FHPVGFADGF EMYDIIARRS
     RLYAYCYPLI ELFLGLAYLS FFLPILTYLL TIVLLSIGAV GVVNALQKGL DIKCPCMGTV
     LDVPLSTVTL TEDIAMAIMA FILLIKSLFT A
//
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