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PPBL_PSEAE
ID   PPBL_PSEAE              Reviewed;         368 AA.
AC   P35482; O52768;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Alkaline phosphatase L {ECO:0000303|PubMed:8454193};
DE            Short=L-AP;
DE            EC=3.1.3.1 {ECO:0000269|PubMed:8454193};
DE   AltName: Full=Low-molecular-weight alkaline phosphatase A {ECO:0000303|PubMed:11985723};
DE   AltName: Full=Protein DING {ECO:0000303|PubMed:18282104};
DE   Flags: Precursor;
GN   Name=lapA {ECO:0000303|PubMed:11985723};
GN   Synonyms=phoA {ECO:0000303|Ref.1}, phoA2 {ECO:0000305}, pstS;
GN   OrderedLocusNames=PA0688;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RA   Schuermann M., Liebeton K., Jaeger K.-E.;
RT   "Cloning and preliminary characterization of phoA encoding alkaline
RT   phosphatase of Pseudomonas aeruginosa.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   PROTEIN SEQUENCE OF 24-37, FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=H103;
RX   PubMed=8454193; DOI=10.1111/j.1574-6968.1993.tb05977.x;
RA   Tan A.S.P., Worobec E.A.;
RT   "Isolation and characterization of two immunochemically distinct alkaline
RT   phosphatases from Pseudomonas aeruginosa.";
RL   FEMS Microbiol. Lett. 106:281-286(1993).
RN   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=11985723; DOI=10.1046/j.1365-2958.2002.02759.x;
RA   Ball G., Durand E., Lazdunski A., Filloux A.;
RT   "A novel type II secretion system in Pseudomonas aeruginosa.";
RL   Mol. Microbiol. 43:475-485(2002).
RN   [5]
RP   INDUCTION.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=18282104; DOI=10.1371/journal.ppat.0040043;
RA   Zaborina O., Holbrook C., Chen Y., Long J., Zaborin A., Morozova I.,
RA   Fernandez H., Wang Y., Turner J.R., Alverdy J.C.;
RT   "Structure-function aspects of PstS in multi-drug-resistant Pseudomonas
RT   aeruginosa.";
RL   PLoS Pathog. 4:E43-E43(2008).
RN   [6]
RP   CRYSTALLIZATION.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=24100568; DOI=10.1107/s1744309113024172;
RA   Djeghader A., Gotthard G., Suh A., Gonzalez D., Scott K., Chabriere E.,
RA   Elias M.;
RT   "Crystallization and preliminary X-ray diffraction analysis of a high-
RT   affinity phosphate-binding protein endowed with phosphatase activity from
RT   Pseudomonas aeruginosa PAO1.";
RL   Acta Crystallogr. F 69:1143-1146(2013).
CC   -!- FUNCTION: Has both a phosphomonoesterase and phosphodiesterase
CC       activity. {ECO:0000269|PubMed:8454193}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC         Evidence={ECO:0000269|PubMed:8454193};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11985723,
CC       ECO:0000269|PubMed:8454193}. Periplasm {ECO:0000269|PubMed:8454193}.
CC       Note=Secreted and to some extent periplasmic (PubMed:8454193).
CC       Secretion is hxc-dependent and xcp-independent (PubMed:11985723).
CC       {ECO:0000269|PubMed:11985723, ECO:0000269|PubMed:8454193}.
CC   -!- DEVELOPMENTAL STAGE: Expressed 7 hours after introduction into
CC       phosphate poor media. {ECO:0000269|PubMed:8454193}.
CC   -!- INDUCTION: Contradictory; shown to be induced in phosphate poor media
CC       (PubMed:8454193). Does not respond to decreased phosphate
CC       (PubMed:18282104). {ECO:0000269|PubMed:18282104,
CC       ECO:0000269|PubMed:8454193}.
CC   -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR   EMBL; AF047381; AAC04870.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG04077.1; -; Genomic_DNA.
DR   PIR; E83559; E83559.
DR   RefSeq; NP_249379.1; NC_002516.2.
DR   RefSeq; WP_003112123.1; NZ_QZGE01000025.1.
DR   AlphaFoldDB; P35482; -.
DR   SMR; P35482; -.
DR   IntAct; P35482; 1.
DR   MINT; P35482; -.
DR   STRING; 287.DR97_1431; -.
DR   PaxDb; P35482; -.
DR   EnsemblBacteria; AAG04077; AAG04077; PA0688.
DR   GeneID; 880790; -.
DR   KEGG; pae:PA0688; -.
DR   PATRIC; fig|208964.12.peg.720; -.
DR   PseudoCAP; PA0688; -.
DR   HOGENOM; CLU_047926_0_0_6; -.
DR   InParanoid; P35482; -.
DR   OMA; KGPKNDG; -.
DR   PhylomeDB; P35482; -.
DR   BioCyc; PAER208964:G1FZ6-698-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IDA:PseudoCAP.
DR   InterPro; IPR024370; PBP_domain.
DR   Pfam; PF12849; PBP_like_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Periplasm; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:8454193"
FT   CHAIN           24..368
FT                   /note="Alkaline phosphatase L"
FT                   /id="PRO_0000031860"
FT   CONFLICT        37
FT                   /note="K -> R (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   368 AA;  37885 MW;  44F3D6BF203098F1 CRC64;
     MFKRSLIAAS LSVAALVSAQ AMAVTGGGAS LPAELYKGSA DSILPANFSY AVTGSGTGKN
     AFLTNNSSLF GTTGTVHYAG SDSVLSGSEL TTYNSNYNGT YGPLIQIPSV ATSVTVPYRK
     DGNTTLNLTS AQLCDAFSGA KTTWGQLLGT TDSTPIRIVY RTGSSGTTEL FTRHLNSICP
     TRFATNSTFT NARLPAGGTL PSNWVGVAAT STVVSTVKAT NGSLGYVSPD AVNINSNAEV
     SRVNGNLPTQ ANVSTALGSV APPANAADRA DPSKWVPVFT NPSAGYSIVG YTNFVFGQCY
     KDASVSTDVR AFINKHYGGT TTNAAVAAHG FIPLTPAWKS AIVSAFYTGT SENLAIGNTN
     VCNTKGRP
 
 
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