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Database: UniProt
Entry: A0A1M5SSQ8_9RHOB
LinkDB: A0A1M5SSQ8_9RHOB
Original site: A0A1M5SSQ8_9RHOB 
ID   A0A1M5SSQ8_9RHOB        Unreviewed;       465 AA.
AC   A0A1M5SSQ8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Probable alginate O-acetylase AlgI {ECO:0000256|ARBA:ARBA00016084};
DE   AltName: Full=Alginate biosynthesis protein AlgI {ECO:0000256|ARBA:ARBA00031030};
GN   ORFNames=SAMN05444003_3084 {ECO:0000313|EMBL:SHH41545.1};
OS   Cognatiyoonia sediminum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cognatiyoonia.
OX   NCBI_TaxID=1508389 {ECO:0000313|EMBL:SHH41545.1, ECO:0000313|Proteomes:UP000184074};
RN   [1] {ECO:0000313|EMBL:SHH41545.1, ECO:0000313|Proteomes:UP000184074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28715 {ECO:0000313|EMBL:SHH41545.1,
RC   ECO:0000313|Proteomes:UP000184074};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FQXB01000007; SHH41545.1; -; Genomic_DNA.
DR   RefSeq; WP_072902622.1; NZ_FQXB01000007.1.
DR   AlphaFoldDB; A0A1M5SSQ8; -.
DR   STRING; 1508389.SAMN05444003_3084; -.
DR   OrthoDB; 139172at2; -.
DR   Proteomes; UP000184074; Unassembled WGS sequence.
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:SF23; TEICHOIC ACID D-ALANYLTRANSFERASE; 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|ARBA:ARBA00023315,
KW   ECO:0000256|PIRNR:PIRNR016636};
KW   Alginate biosynthesis {ECO:0000256|ARBA:ARBA00022841};
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:UP000184074};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, 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        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        47..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        310..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        409..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        437..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   465 AA;  51992 MW;  4EF167CCE271363C CRC64;
     MVFSSLIFIF GFLPAFLAVY YVVPARFRSA WILIGSYAFY GWWRLEYLAV VVGISLVSFI
     CANAALAAKS KKRKSLWVKL GVGTDLAVLG YFKYTYFIAE SIDAALISFD GASLGVEKIV
     LPIGISFLTF QSISYILDVS RKDAPPARTV MDFLAFSALF PQLIAGPVLR YKDVADQFQS
     RTHSLLVFQS GCKRFVQGLA MKLLIADTVA PLADRMFALD APTMAEAWLG AGAYSIQLLF
     DFAGYSAMAI GLGLMIGFRF VENFNAPYIS QSVTEFWRRW HISLSNWLRD YLYIPLGGNR
     GGTLKTFRNL MLTMVLGGFW HGANWTFIIW GAWHGLLLSL ERAIGSKSRK RVWPRYTGWP
     FTMVAVIVGW VMFRAATVTD AFEMYRGMVG LNGINISAET IYFNQPIEFV GLIVGAILSI
     APSINPRVSV PQYLMSLQLF TPLMFVGCTI VLSARAHSPF LYFQF
//
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