ID A0A1B1NC16_9MICO Unreviewed; 278 AA.
AC A0A1B1NC16;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Phosphoesterase, PA-phosphatase related {ECO:0000313|EMBL:ANS78979.1};
GN ORFNames=SGUI_1583 {ECO:0000313|EMBL:ANS78979.1};
OS Serinicoccus hydrothermalis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=1758689 {ECO:0000313|EMBL:ANS78979.1, ECO:0000313|Proteomes:UP000092482};
RN [1] {ECO:0000313|EMBL:ANS78979.1, ECO:0000313|Proteomes:UP000092482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT9 {ECO:0000313|EMBL:ANS78979.1,
RC ECO:0000313|Proteomes:UP000092482};
RA Tang K.;
RT "Shallow-sea hydrothermal system.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP014989; ANS78979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1NC16; -.
DR STRING; 1758689.SGUI_1583; -.
DR KEGG; serj:SGUI_1583; -.
DR Proteomes; UP000092482; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd03392; PAP2_like_2; 1.
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 SMART; SM00014; acidPPc; 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:UP000092482};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..209
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 232..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 278 AA; 30378 MW; E838A277FD4BC8B1 CRC64;
MVSFRRLTSL PVLIGALVLV TYLAAAPLRE FDRSLHGFWS DELTPRWTDF LDQVPNAVAG
QAVCLPVLLL VAFTLAWKHR TWRPVLIAGA TEAGFYGVVG GLKLVLARTS PKADDVSGRF
FNGGAEEHGW YGMTYPSGHA AEAILIYGAA AYLLVVYSRP DSRLRRRLGW AMTLITINAV
AVAYYLGYHW PSDLIGGMLT GAVVLRVIID VDQWLARRRA RAAWQRLERT REAAPVAPRP
APTPVGAASP AAAPAPVPPR IPAGHGHREH DREPELVP
//
