GenomeNet

Database: UniProt
Entry: A0A1R1QK50_9BACI
LinkDB: A0A1R1QK50_9BACI
Original site: A0A1R1QK50_9BACI 
ID   A0A1R1QK50_9BACI        Unreviewed;       621 AA.
AC   A0A1R1QK50; A0A1R1RY29;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Acetyltransferase {ECO:0000313|EMBL:OMI05047.1};
GN   ORFNames=BTA30_11055 {ECO:0000313|EMBL:OMI30926.1}, BW143_12575
GN   {ECO:0000313|EMBL:OMI05047.1};
OS   Bacillus swezeyi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1925020 {ECO:0000313|EMBL:OMI05047.1, ECO:0000313|Proteomes:UP000187367};
RN   [1] {ECO:0000313|EMBL:OMI05047.1, ECO:0000313|Proteomes:UP000187367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-41282 {ECO:0000313|EMBL:OMI05047.1,
RC   ECO:0000313|Proteomes:UP000187367}, and NRRL B-41294
RC   {ECO:0000313|EMBL:OMI30926.1, ECO:0000313|Proteomes:UP000187536};
RA   Dunlap C.;
RT   "Bacillus phylogenomics.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC   -!- SIMILARITY: Belongs to the acyltransferase 3 family.
CC       {ECO:0000256|ARBA:ARBA00007400}.
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:OMI05047.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MTJL01000023; OMI05047.1; -; Genomic_DNA.
DR   EMBL; MRBK01000011; OMI30926.1; -; Genomic_DNA.
DR   RefSeq; WP_076761302.1; NZ_MTJL01000023.1.
DR   OrthoDB; 9796461at2; -.
DR   Proteomes; UP000187367; Unassembled WGS sequence.
DR   Proteomes; UP000187536; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd01840; SGNH_hydrolase_yrhL_like; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR23028; ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR23028:SF53; ACYL_TRANSF_3 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01757; Acyl_transf_3; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:OMI30926.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        206..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..344
FT                   /note="Acyltransferase 3"
FT                   /evidence="ECO:0000259|Pfam:PF01757"
FT   REGION          415..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  70349 MW;  1EB5A64FB6AE0749 CRC64;
     MLDQTQHHRY IPGLDGLRAF AVLAVIAYHL DFNWANGGFI GVDIFFVLSG YLITSIILPA
     YGNDITLSFR DFWLRRMRRL LPAAVLMIIA TVIWTVLFNR ELMHTVRGDA ASSLLYVSNW
     WFIFHNLSYF DSFGSPSPLK NLWSLAIEEQ FYIVWPILLL FGMYILKKRE RLAVAVLLLA
     LGSAVWMSVL YVPGGDPSRV YYGTDTRAFE LLSGCALALV WPMKRLSSNR LPNKLKHALH
     RTELAALAFL ILCIYFVDEY APFLYHGGML LISLFAAVFI ACVSHPISFV GYLLSWKPLR
     WIGTRSYGIY LWHYPVIVLS TPVQEIGNPV YWHAAVKVAV TLILAEASYR FIEKPIREDG
     FRPFFRAVFL NKWLEWKTSS VLNKVSMGLM IAALLIFAGG LSGLADEKQQ PQWTYSKSYQ
     ETSAAPDQAS DQNEEEKDEK TKTDENQDQA ETSDQQTKEN QDQQPPNRSE KEVLAIGDSV
     MLDIASNLRH RLPGITIDGK VGRQVSPALQ LTSAYESFNQ PDKAVIIELG TNGYFTDGQM
     DALLNAFSKA DIYLVNTRVP RQWESKVNES LKRQANNRKN VTLVDWHSEA LQHPEYFTSD
     GVHLVPKGAE ALADLIVQAM K
//
DBGET integrated database retrieval system