ID M2NCW3_9FIRM Unreviewed; 228 AA.
AC M2NCW3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|Pfam:PF01569};
GN ORFNames=HMPREF9943_01685 {ECO:0000313|EMBL:EMD16013.1};
OS Eggerthia catenaformis OT 569 = DSM 20559.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Eggerthia.
OX NCBI_TaxID=999415 {ECO:0000313|EMBL:EMD16013.1, ECO:0000313|Proteomes:UP000011758};
RN [1] {ECO:0000313|EMBL:EMD16013.1, ECO:0000313|Proteomes:UP000011758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT 569 {ECO:0000313|EMBL:EMD16013.1,
RC ECO:0000313|Proteomes:UP000011758};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Mathney J., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lactobacillus catenaformis F0143.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:EMD16013.1}.
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DR EMBL; AGEJ01000025; EMD16013.1; -; Genomic_DNA.
DR AlphaFoldDB; M2NCW3; -.
DR STRING; 999415.HMPREF9943_01685; -.
DR PATRIC; fig|999415.3.peg.1712; -.
DR eggNOG; COG0671; Bacteria.
DR BioCyc; ECAT999415-HMP:GTTI-1747-MONOMER; -.
DR Proteomes; UP000011758; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011758};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..217
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|Pfam:PF01569"
SQ SEQUENCE 228 AA; 27072 MW; 0EF3DEA55634CF62 CRC64;
MLVWAKGDYM NKLKELINKY KHVWIVVVYF IFYLPWYFGI QQRDPSRFFD MHVTLDSMIS
FKPIFIFAYM YWFIFVAATF LFVFFYDKDE FYKCCAFMFG GMTICLIIFT FFPTTFDYRP
AVISGNYLER FFLNIVYTAD KPTNVFPSIH VLNSIGCAIV LIKSKYFKNN YLMYTFAIMS
AVIITLSTMF VKQHSIMDAL AAGIISVILY YLVYVVFDGY LKREHHES
//
