ID   A0A261G1K9_9BIFI        Unreviewed;       969 AA.
AC   A0A261G1K9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Acid phosphatase {ECO:0000313|EMBL:OZG64876.1};
GN   ORFNames=BHAP_0813 {ECO:0000313|EMBL:OZG64876.1};
OS   Bifidobacterium hapali.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1630172 {ECO:0000313|EMBL:OZG64876.1, ECO:0000313|Proteomes:UP000216074};
RN   [1] {ECO:0000313|EMBL:OZG64876.1, ECO:0000313|Proteomes:UP000216074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100202 {ECO:0000313|EMBL:OZG64876.1,
RC   ECO:0000313|Proteomes:UP000216074};
RX   PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA   Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA   Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA   van Sinderen D., Ventura M.;
RT   "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT   family.";
RL   BMC Genomics 18:568-568(2017).
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:OZG64876.1}.
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DR   EMBL; MWWY01000018; OZG64876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261G1K9; -.
DR   OrthoDB; 9805301at2; -.
DR   Proteomes; UP000216074; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR   CDD; cd03397; PAP2_acid_phosphatase; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 2.
DR   InterPro; IPR001011; Acid_Pase_classA_bac.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR14969:SF13; AT30094P; 1.
DR   PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR   Pfam; PF01569; PAP2; 2.
DR   PRINTS; PR00483; BACPHPHTASE.
DR   SMART; SM00014; acidPPc; 2.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..969
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012559940"
FT   TRANSMEM        944..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          153..302
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   DOMAIN          568..709
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          879..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   969 AA;  102229 MW;  B9FCC77A228127C0 CRC64;
     MNTTSRKSTV VKGAVAGIAA LAMLLTGGVA ANAAESSAFG NAVKPDITGL LSQYYDWWTP
     KKVVNNTPEG DAFRGNVTDA GTSVLDQNDK TVVTINNKAA SDTTKVDGKY TQAERAALDA
     SDGDALRIYK DAFGPVIGQY VADGLAQGKL PKTNDLVFNN DSDIAFAKFV GTGSAKKDFN
     YPRPYFSVDK EGVDRTLGGS NNLNGLASTL NIKRIPLITI DGQEYGEDYT DYQEPSQSFP
     SGHTTKTYNR GIGLATLLPE LGPELAARAA EGGNNRVVLG VHYPMDVIGG RISATASLTA
     LWSDPTFRTN ELLPAHDELE NYIASRCAAD GYGDTVAKCV DKLGANDDKG YVNTFTDAVS
     TEPVTDRESA IDAYTARMTY GFKQVSAAGQ APVVPDGAEN LLLTAFPTLT DDQRKAVLAA
     SEIDSGYPLD ASSEGFQRIN LAKAFSAKVT LDESGKTITA ISFGNSAPTV VKTPSSKDAI
     TNLLTDFNKY FVAGVGVTDE GKSVLEHDDE LTESINNKAF GTDGKTEQDQ RALSDAQMNS
     TNTLYDALGP VLGKYYKDAA DAGKLPQTEA YLEKMDESAS TSVAKATYQH PRPYVDRVNF
     NGTTLNMNGT KQTLNIKKVP GYENFDWGDG EPLDNEYDGL YNSGSFPSGH TTYAFTQGVG
     LANILPELGT EIMTRVSEAG NNRIVLGVHY PLDIMGGHIA GQSGVAAALN DPDTQKQAAD
     ARTELVNYLT AQCKADKHGD TLEDCITNTG ANANKGYTNE FTDDVSKAPV TDRASALTAY
     TARMTYGFEQ TGKAGQAPVV PDDAVNLLSN VAAFRNLTVD QKKAVIAASE IDSGYPLDAS
     SEGWGRVNLA AVYSSKVTLD KAGKVVKVEP GQAQASVVTV SDNTNHGGNG GNTNGGNTNG
     GNTNNGGQNQ QNNNQNNNQN NGGDNQANKP NTTPKKLANT GANVSGIVIA LAALAVAGGA
     AVMLRKRNA
//