ID A0A1M5ZFC3_9FIRM Unreviewed; 662 AA.
AC A0A1M5ZFC3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains {ECO:0000313|EMBL:SHI22623.1};
GN ORFNames=SAMN02745823_03611 {ECO:0000313|EMBL:SHI22623.1};
OS Sporobacter termitidis DSM 10068.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Sporobacter.
OX NCBI_TaxID=1123282 {ECO:0000313|EMBL:SHI22623.1, ECO:0000313|Proteomes:UP000183995};
RN [1] {ECO:0000313|EMBL:SHI22623.1, ECO:0000313|Proteomes:UP000183995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10068 {ECO:0000313|EMBL:SHI22623.1,
RC ECO:0000313|Proteomes:UP000183995};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQXV01000018; SHI22623.1; -; Genomic_DNA.
DR RefSeq; WP_073082448.1; NZ_FQXV01000018.1.
DR AlphaFoldDB; A0A1M5ZFC3; -.
DR STRING; 1123282.SAMN02745823_03611; -.
DR Proteomes; UP000183995; Unassembled WGS sequence.
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 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; O-ACYLTRANSFERASE HOMOLOG; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:SHI22623.1};
KW Hydrolase {ECO:0000313|EMBL:SHI22623.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000183995};
KW Transferase {ECO:0000313|EMBL:SHI22623.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..347
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
FT REGION 417..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..496
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 72365 MW; 773909498B7FDA84 CRC64;
MRYNTIQKRS YMPGLDGLRA LAVVAVIGYH LGLPFLPGGF LGVTLFFALS GYLITDILMS
EWARESKISL KNFFIRRGKR LLPAVIFLLL CVSAYVSLFR PDLLSNLKSA FLPALFFFSN
WWYIFNGTPY FASFATPSLL THFWSLAVEA QFYLIWPLLL IAGQRFIKKK WLMIALTALA
AAASAVLMAV LFQPGVDPSR IYYGTDTRVF SLLLGACLAL ACPSRKIMEA GRSRTARIVL
DVAGFAALLG ILFAVIYFTQ YDDILYRGGM FLFSVVSLLL IAAAATPSTI IGKFFSIKPL
RFIGNISYGI YLWQFPVIVI SNTVFGSDRV NVPLSICQVA ATVLLAAFSY YAVERPIRKN
RIDDLLRNDI YMKILHARWW KKTAGALAVA LVVVAGVGLL YARPVDNRDE ELSALPSELH
MDPSNDPDTA PPPADTSTAP PSAEVSPSAP ATPDDSPDMS PTPPGVKPSD KPSPPPSPEG
TDPAQSPSPP PAASPTDSAP IVSSDLSVTL IGDSIGIDVA PYLKKYYPNM IAEAKVGRQF
YEAKKVITEL IQNDQLAPTV IIELGSNGTV KESSLRDIID LIGSDRKIVF VNTQVPKSWC
TAVNSTLSKV SEEYANTVVA DWYGASVNKS EYFYKDDVHP NKAGSLVLAK VISDAIENLH
NM
//
