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PHNE_MYCS2
ID   PHNE_MYCS2              Reviewed;         532 AA.
AC   A0QQ68; I7G248;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Phosphate-import permease protein PhnE;
GN   Name=phnE; OrderedLocusNames=MSMEG_0646, MSMEI_0630;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   INVOLVEMENT IN PHOSPHATE ASSIMILATION, AND GENE NAME.
RX   PubMed=15758213; DOI=10.1099/mic.0.27624-0;
RA   Tran S.L., Rao M., Simmers C., Gebhard S., Olsson K., Cook G.M.;
RT   "Mutants of Mycobacterium smegmatis unable to grow at acidic pH in the
RT   presence of the protonophore carbonyl cyanide m-chlorophenylhydrazone.";
RL   Microbiology 151:665-672(2005).
RN   [5]
RP   FUNCTION IN PHOSPHATE TRANSPORT, AND INDUCTION.
RX   PubMed=17074913; DOI=10.1099/mic.0.29201-0;
RA   Gebhard S., Tran S.L., Cook G.M.;
RT   "The Phn system of Mycobacterium smegmatis: a second high-affinity ABC-
RT   transporter for phosphate.";
RL   Microbiology 152:3453-3465(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex PhnCDE involved in
CC       phosphate import. Responsible for the translocation of the substrate
CC       across the membrane. {ECO:0000269|PubMed:17074913}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PhnC),
CC       two transmembrane proteins (PhnE) and a solute-binding protein (PhnD).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- INDUCTION: By phosphate-limited conditions, via derepression by PhnF,
CC       and probably also via the two-component regulatory system senX3/regX3.
CC       {ECO:0000269|PubMed:17074913}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; CP000480; ABK75678.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP37111.1; -; Genomic_DNA.
DR   RefSeq; WP_011727091.1; NZ_SIJM01000009.1.
DR   RefSeq; YP_885056.1; NC_008596.1.
DR   AlphaFoldDB; A0QQ68; -.
DR   SMR; A0QQ68; -.
DR   STRING; 246196.MSMEI_0630; -.
DR   TCDB; 3.A.1.9.2; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; ABK75678; ABK75678; MSMEG_0646.
DR   EnsemblBacteria; AFP37111; AFP37111; MSMEI_0630.
DR   GeneID; 66738824; -.
DR   KEGG; msg:MSMEI_0630; -.
DR   KEGG; msm:MSMEG_0646; -.
DR   PATRIC; fig|246196.19.peg.642; -.
DR   eggNOG; COG3639; Bacteria.
DR   OMA; YRFECAL; -.
DR   OrthoDB; 426495at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0015416; F:ABC-type phosphonate transporter activity; IEA:InterPro.
DR   GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR   CDD; cd06261; TM_PBP2; 2.
DR   Gene3D; 1.10.3720.10; -; 2.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR005769; PhnE/PtxC.
DR   Pfam; PF00528; BPD_transp_1; 2.
DR   SUPFAM; SSF161098; SSF161098; 2.
DR   TIGRFAMs; TIGR01097; PhnE; 2.
DR   PROSITE; PS50928; ABC_TM1; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Phosphate transport; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..532
FT                   /note="Phosphate-import permease protein PhnE"
FT                   /id="PRO_0000357469"
FT   TRANSMEM        23..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        85..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        134..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        187..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        216..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        245..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        287..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        345..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        395..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        452..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        478..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        505..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          81..264
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          341..524
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  55928 MW;  411F7E36201A62A3 CRC64;
     MTTEITRPPA PPSRPSESRK PSLPGLLHLV AIAAVLATIV SAWAIDFVPT ALIDGSDNIV
     ALLQRMIPPR LDDPARIGML AVETLLMAVL GTTLAAIASV PLAFLAARNT TPHPAVQAVA
     RAVITFCRAM PDLLFAVLFV RALGIGVLPG VLALALHSIG MLGKVFADAI EQTDAGPREA
     VRSTGVGYFR ELLNAVVPQV VPSWIAMFVY RIDINLRMSV VLGFVGAGGI GFALQDALRG
     LIYPRALGIV CVILVIIAGM ELLAIAIRRI LLDPSRSNPL RDRIARFGLS GVLVGSCVAA
     FVLLKINPLA LFTWVFPSVG IFTRMVPPNF DALGVDLFTA AAQTVAIGVV ATAIGIALSI
     PAGILAARNV SPHPALYWPA RAWILVVRAV PELILAVVFV AALGLGPIAG TCALAIGSIG
     FLAKLVADAV EEIDPGPMEA VRSVGGGWWK TLFAAVLPQS MPALVGSSLY LFDVNVRTST
     ILGIVGAGGV GYLLFESIRT LNFDVAGAIV IVIFVIVYAI ERLSGWIRSR LV
 
 
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