ID I0JJF7_HALH3 Unreviewed; 374 AA.
AC I0JJF7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Acyltransferase 3 {ECO:0000313|EMBL:CCG44275.1};
GN OrderedLocusNames=HBHAL_1913 {ECO:0000313|EMBL:CCG44275.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG44275.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG44275.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family.
CC {ECO:0000256|ARBA:ARBA00007400}.
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DR EMBL; HE717023; CCG44275.1; -; Genomic_DNA.
DR AlphaFoldDB; I0JJF7; -.
DR STRING; 866895.HBHAL_1913; -.
DR KEGG; hhd:HBHAL_1913; -.
DR PATRIC; fig|866895.3.peg.914; -.
DR eggNOG; COG1835; Bacteria.
DR HOGENOM; CLU_047714_1_0_9; -.
DR Proteomes; UP000007397; Chromosome.
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 InterPro; IPR002656; Acyl_transf_3_dom.
DR PANTHER; PTHR40074; O-ACETYLTRANSFERASE WECH; 1.
DR PANTHER; PTHR40074:SF2; O-ACETYLTRANSFERASE WECH; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:CCG44275.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007397};
KW Transferase {ECO:0000313|EMBL:CCG44275.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..336
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
SQ SEQUENCE 374 AA; 44090 MW; F2AAE961D91CE23D CRC64;
MQKDRIESIY FLRLFAMLMV VLVHTTGIFQ SVFSEGSMEF GVYHFINRII RLEAGIFIMI
TAMVFFYKYI DKKMTVPELK DYYKKRALYI VVPYLLWALF YEAFSLYIGA VPLNFAEMTW
RIIQGESFYQ LHFIFLIVQF YLVFPIILFV AQKVPVFKKY MWVFGIAIEI GYYFFDQTFK
LIPFSIFLSS LGPYLLGAWI GTYYKEQRSL IYRKTNVAWA VFALAAGVTT VFLHYHLYTV
STFVLPGYVY LIMNLSYILS GSYILFRLTE VVCDKWPAII PYVQRVAVYS FGFYLLHPFI
LKLVAQFIPA PEGYWFHLFI LLRYVSTIVL CYLVIWFTHK YFVRPGLLFG KLPRRAPSIL
ETPKVSTENK RTGT
//
