ID A9F165_SORC5 Unreviewed; 541 AA.
AC A9F165;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:CAN91336.1};
DE EC=3.1.4.1 {ECO:0000313|EMBL:CAN91336.1};
GN Name=phoD {ECO:0000313|EMBL:CAN91336.1};
GN OrderedLocusNames=sce1179 {ECO:0000313|EMBL:CAN91336.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN91336.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN91336.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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DR EMBL; AM746676; CAN91336.1; -; Genomic_DNA.
DR AlphaFoldDB; A9F165; -.
DR STRING; 448385.sce1179; -.
DR KEGG; scl:sce1179; -.
DR eggNOG; COG3540; Bacteria.
DR HOGENOM; CLU_015982_1_0_7; -.
DR OMA; YEHMPIR; -.
DR OrthoDB; 327733at2; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR CDD; cd07389; MPP_PhoD; 1.
DR Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR018946; PhoD-like_MPP.
DR InterPro; IPR038607; PhoD-like_sf.
DR InterPro; IPR032093; PhoD_N.
DR PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR PANTHER; PTHR43606:SF2; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR Pfam; PF09423; PhoD; 1.
DR Pfam; PF16655; PhoD_N; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CAN91336.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..541
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002738505"
FT DOMAIN 57..145
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 156..492
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
FT REGION 31..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 59198 MW; F277A9F05FC6A115 CRC64;
MSMARRSILC SVSMFSLAAL PGLSGGWGAA PDGDAPLPAS GDAPSPASEV SKTVFQHGVA
SGDPLPDAVI LWTRVTAGKA GAVAVTWQIA LDAGFTRIVG SGALLTDEER DHTVKVDAGG
LDPGKTYYYR FIALGGSSPV GRTRTAPRGR AGRLRFAVAS CASYAHGLFH GYRHIAARLD
LDAVIHLGDY IYEFGAGQYG SARHYEPAHE IVTLADYRAR YAQYRRDRDL QAAHQQHPFI
TVWDDHELAN NTWKGGAGNH AWPAEGAWEE RRAVAQRAYA EWMPIRERGE ELRCAGRIWR
ALRYGDLVDL FLLDTRAWGR DRQADPGDRA AIEAPARTIL GRDQEAWLRA ELAGSTAAWK
VIGQQVLMGQ LPQDLNTDAW DGYPAARQRF FELLDEERVR DVVVLSGDTH ASWAIDLAPA
PLDPARYDAA TGRGALAVEI AVPGITSPWL TEEQARAAEP LFLANPHVQY ADLWRRGYAI
LDVTPERVQG AWFLYDAPER PQVDEVFAAA FAARRGESHL RREEAAALAI DDPPEAAPRV
S
//