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Database: UniProt
Entry: K2JUL3_9RHOB
LinkDB: K2JUL3_9RHOB
Original site: K2JUL3_9RHOB 
ID   K2JUL3_9RHOB            Unreviewed;       301 AA.
AC   K2JUL3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Acyltransferase domain-containing protein {ECO:0000313|EMBL:EKE74064.1};
GN   ORFNames=B30_00020 {ECO:0000313|EMBL:EKE74064.1};
OS   Celeribacter baekdonensis B30.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE74064.1, ECO:0000313|Proteomes:UP000006762};
RN   [1] {ECO:0000313|EMBL:EKE74064.1, ECO:0000313|Proteomes:UP000006762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B30 {ECO:0000313|EMBL:EKE74064.1,
RC   ECO:0000313|Proteomes:UP000006762};
RA   Wang W.;
RT   "Celeribacter baekdonensis B30 Genome Sequencing.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:EKE74064.1}.
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DR   EMBL; AMRK01000001; EKE74064.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2JUL3; -.
DR   STRING; 1208323.B30_00020; -.
DR   PATRIC; fig|1208323.3.peg.3; -.
DR   eggNOG; COG0204; Bacteria.
DR   Proteomes; UP000006762; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07986; LPLAT_ACT14924-like; 1.
DR   InterPro; IPR045746; ACT14924-like_Acyltransf_dom.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF19576; Acyltransf_2; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:EKE74064.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006762};
KW   Transferase {ECO:0000313|EMBL:EKE74064.1}.
FT   DOMAIN          107..230
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   301 AA;  33651 MW;  4B52BC0D3AB8A4E7 CRC64;
     MAHPQDQATE TQVTEPHVPK PGDADFIKYD GRRLSYAGTY SDPSKVVVIR SIEWITGKLP
     LLRRIRRFER MGTPMGQPFF SQALEVMGID VTTPEEQISK IPATGPLVVV ANHPHGLVDG
     LVMAELIGKV RTDYKILTRS LLTGIREIDP FMLPVPFPHE EDSHRKSILM RNEAMDTLKA
     GGVIILFPAG AVASSETWFG PVKEKEWNPF TAKMVLKSGA TVLPIYFPGR NTRLYQIADK
     ISATIRQGLL LHEIVHALNK PQSPIIGDPL SPDDLNDWQK KTREFMAWMR THTLALGGRT
     D
//
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