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Database: UniProt
Entry: A0A1X6WSU0_9MICO
LinkDB: A0A1X6WSU0_9MICO
Original site: A0A1X6WSU0_9MICO 
ID   A0A1X6WSU0_9MICO        Unreviewed;       367 AA.
AC   A0A1X6WSU0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Phosphoesterase, PA-phosphatase related {ECO:0000313|EMBL:SLM87980.1};
GN   ORFNames=FM110_00790 {ECO:0000313|EMBL:SLM87980.1};
OS   Brachybacterium nesterenkovii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=47847 {ECO:0000313|EMBL:SLM87980.1, ECO:0000313|Proteomes:UP000195981};
RN   [1] {ECO:0000313|EMBL:SLM87980.1, ECO:0000313|Proteomes:UP000195981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP104813 {ECO:0000313|EMBL:SLM87980.1,
RC   ECO:0000313|Proteomes:UP000195981};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FWFG01000010; SLM87980.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6WSU0; -.
DR   OrthoDB; 3240395at2; -.
DR   Proteomes; UP000195981; 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   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195981};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..367
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039427313"
FT   TRANSMEM        58..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        329..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..197
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          212..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  37754 MW;  55F28122C615DBA3 CRC64;
     MTRGAIALRL LGALLASAAS IAACWALAKA AVHTARGQRL DQLVLTAAQN DTGPMTRIVF
     PVLNTVTVPV IVAAILVAVV LALLQRRASM VVHLVVLVAG AAATTQVVKH LVIDRTALAP
     GLDVTPNSFP SGHTTLAAAV AIALMLASPR HIRSLVALLG AAWTAVAGIG TIAGGWHRPS
     DVLGALLVVG AWTFLVLAVD AVLAMIRARA PEPDAEDHPH DGHDDDLGRD GTAEPPRPAT
     WDDPDPVWDE EAQMWVAGHS APAHEGAAAR PRRDRRRRAR SLLPVHSNGR VAAALLSVGS
     VLGVIVGAVL LATVPTPLDL ASASAQARAY AATIGIVGGA TAALFAVTLL VHVPALPSSS
     ADPVRVR
//
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