ID Q897X8_CLOTE Unreviewed; 470 AA.
AC Q897X8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Alginate O-acetylation protein {ECO:0000313|EMBL:AAO35208.1};
GN OrderedLocusNames=CTC_00592 {ECO:0000313|EMBL:AAO35208.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO35208.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO35208.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010323, ECO:0000256|PIRNR:PIRNR016636}.
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DR EMBL; AE015927; AAO35208.1; -; Genomic_DNA.
DR RefSeq; WP_011098874.1; NC_004557.1.
DR AlphaFoldDB; Q897X8; -.
DR STRING; 212717.CTC_00592; -.
DR GeneID; 24253438; -.
DR KEGG; ctc:CTC_00592; -.
DR HOGENOM; CLU_025255_1_3_9; -.
DR OrthoDB; 9805788at2; -.
DR Proteomes; UP000001412; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:InterPro.
DR InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB.
DR InterPro; IPR028362; AlgI.
DR InterPro; IPR004299; MBOAT_fam.
DR PANTHER; PTHR13285; ACYLTRANSFERASE; 1.
DR PANTHER; PTHR13285:SF18; PROTEIN-CYSTEINE N-PALMITOYLTRANSFERASE RASP; 1.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF500217; AlgI; 1.
DR PIRSF; PIRSF016636; AlgI_DltB; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|PIRNR:PIRNR016636};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR016636};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR016636};
KW Reference proteome {ECO:0000313|Proteomes:UP000001412};
KW Transferase {ECO:0000256|PIRNR:PIRNR016636};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 48..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 470 AA; 55322 MW; 79EF8951D3ED6078 CRC64;
MVFSSLVFIF VFLPITLLTY YISPKKLRNL ILLIASLIFY AWGEPIYIFL MMFTTVFSYF
SSLFIDKYKN RKGTSLALFI LSVMVNLGIL CFFKYYGFFI DNINNLFSMN INVKKLPLPV
GISFYTFQTL SYVIDVYLEK VPVQKNIISF STYVTMFPQL VAGPIVKYGD INKQLDNRKE
SLDKFGDGVS YFIRGLSKKV LLANNLGLLW TTVKATSFTE LSIFSAWLGI IAFTLQIYFD
FSGYSDMAIG LGKFFGFELM ENFNYPYISR SVTEFWRRWH ISLGSWFREY VYIPLGGNRT
GAIRQYRNLF IVWFLTGFWH GSNWNFIIWG LYFGVFITLE KVFILKWLNK IPKFISHFYT
LIILIVGWAI FEFENTSLMF SYIKTMFGMG SNPLIDNQSI YYLYTNLFLF MLAIIFSTPL
PKKLFQRFIY NIKLRSFSKL IVPIIYLILI FLCTTYLVNE TYNPFLYFKF
//
