ID A0A1H0SBF3_9ACTN Unreviewed; 705 AA.
AC A0A1H0SBF3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains {ECO:0000313|EMBL:SDP39141.1};
GN ORFNames=SAMN04515671_4014 {ECO:0000313|EMBL:SDP39141.1};
OS Nakamurella panacisegetis.
OC Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC Nakamurella.
OX NCBI_TaxID=1090615 {ECO:0000313|EMBL:SDP39141.1, ECO:0000313|Proteomes:UP000198741};
RN [1] {ECO:0000313|EMBL:SDP39141.1, ECO:0000313|Proteomes:UP000198741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4-7,KCTC 19426,CECT 7604 {ECO:0000313|Proteomes:UP000198741};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR EMBL; LT629710; SDP39141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0SBF3; -.
DR STRING; 1090615.SAMN04515671_4014; -.
DR OrthoDB; 3404679at2; -.
DR Proteomes; UP000198741; Chromosome i.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR InterPro; IPR043968; SGNH.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR23028; ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR23028:SF53; O-ACYLTRANSFERASE HOMOLOG; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
DR Pfam; PF19040; SGNH; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:SDP39141.1};
KW Hydrolase {ECO:0000313|EMBL:SDP39141.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198741};
KW Transferase {ECO:0000313|EMBL:SDP39141.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 56..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..357
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
FT DOMAIN 464..690
FT /note="SGNH"
FT /evidence="ECO:0000259|Pfam:PF19040"
SQ SEQUENCE 705 AA; 74539 MW; AE0FEEA9C3C5B995 CRC64;
MSSPPRPGEP RPAGAGGLTV LGDRRFRPDI QGLRTVAVLL VVLYHCAVPV VRGGYVGVDV
FFVISGFLIT RQLITEHHRA GRVSLSSFYA RRIKRLLPMA LTVVLCTEVA ARFFGPALQS
ATVARDGIFA TFYLMNFRLA TQGIDYQNAG GPVSPLQHFW SLAVEEQFYI GWPLIIVLLG
LAFRGRTRTA ALTVAGLVGV GSLLISIVDT RQNPALAYFA IQTRAWELAV GAAIALATPM
LLRLPQRFGN AASWVGLLLI GASAVFFTDA TQFPGAAAAV PVGGAALIVA AGLKTTAGSA
QWFLGRPAMQ FGGRMSYGWY LWHWPLIVLA PSILATTHGW WGNVVVAAAA LGLSVISYHV
IEAPVARRPV RRGRWFAIGA GLSIVVTAAA VLITVLPTAG LYNSGPAAAL QLGGADAAAL
TAELQRAYDR PEVPSNLAPT LTDAVHDVPV TSSDGCHAEF LAVTVPLCVF GDPAGTRTIV
LFGDSHAQQW FGGLDALARS RGWRLVSWTK AACPLADALF YNAQLERPYS ECTAWRSATI
AKIAALDPDL VVASGADALP GPAYSNRTWA AQTTTSLSAL KRAARQVVFL ADTPLPGTNV
PVCLAANIRT PQNCQFTRRS QTSGATEQNQ QPARHAAVVS AAAADGVAVV DPTDWFCSAT
GCPAVVADTL LYRDATHITQ AYSTALAPVL GRGLAAVVPW IARGR
//
