ID   A0A1V9UUK9_9PSED        Unreviewed;       522 AA.
AC   A0A1V9UUK9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Probable alginate O-acetylase {ECO:0000256|PIRNR:PIRNR016636};
DE            EC=2.3.1.- {ECO:0000256|PIRNR:PIRNR016636};
GN   ORFNames=BWR59_09765 {ECO:0000313|EMBL:OQR33608.1};
OS   Pseudomonas sp. Bc-h.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1943632 {ECO:0000313|EMBL:OQR33608.1, ECO:0000313|Proteomes:UP000192462};
RN   [1] {ECO:0000313|EMBL:OQR33608.1, ECO:0000313|Proteomes:UP000192462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bc-h {ECO:0000313|EMBL:OQR33608.1,
RC   ECO:0000313|Proteomes:UP000192462};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005182, ECO:0000256|PIRNR:PIRNR016636}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|PIRNR:PIRNR016636}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00010323, ECO:0000256|PIRNR:PIRNR016636}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQR33608.1}.
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DR   EMBL; MUIN01000005; OQR33608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9UUK9; -.
DR   STRING; 1943632.BWR59_09765; -.
DR   OrthoDB; 139172at2; -.
DR   UniPathway; UPA00286; -.
DR   Proteomes; UP000192462; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniRule.
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; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|PIRNR:PIRNR016636};
KW   Alginate biosynthesis {ECO:0000256|ARBA:ARBA00022841,
KW   ECO:0000256|PIRNR:PIRNR016636};
KW   Cell inner membrane {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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR016636};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|PIRNR:PIRNR016636};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        354..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        402..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        497..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   522 AA;  59128 MW;  41B290FE152A1711 CRC64;
     MVFSSNVFLF LFLPVFLGLY YLSGQRYRNL LLLIASYVFY AWWRVDFLAL FAGVTLWNYW
     IGLRVGAAGV RTKPAQRWLL LGVAVDLCIL GYFKYANFGV DSINAMMTSV GLQPFILTHV
     LLPIGISFYI FESISYIIDV YRGDTPATRN LIDFAAFVAI FPHLIAGPVL RFRDLVDQFN
     NRTHTLDKFS EGCTRFMQGF IKKVFIADTL AVVADHCFAL QNPTTGDAWL GALAYTAQLY
     FDFSGYSDMA IGLGLMMGFR FMENFKQPYV SQSITEFWRR WHISLSTWLR DYLYITLGGN
     RGGKVATYRN LFLTMLLGGL WHGANITYIV WGAWHGVWLA IEKALGINTT PRTFNVVRWA
     FTFLLVVMGW VIFRAENLHV AARMYGAMFS FSEWQLSDLN RASLTGLQVA TLIVAYITLA
     FFGLRDFYQN RTPAKPTSNE KPVQADGPAT AQPGLIKAVP GDKPGSIHQP GYIVGTEAQV
     QPAYWTADWS RYVMRALILL MFVASILKLS AASFSPFLYF QF
//