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PHAP_SYNY3
ID   PHAP_SYNY3              Reviewed;          89 AA.
AC   P73545;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Phasin PhaP {ECO:0000303|PubMed:25911471};
DE   AltName: Full=GA13 {ECO:0000303|PubMed:9683655};
GN   Name=phaP {ECO:0000303|PubMed:25911471}; OrderedLocusNames=ssl2501;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-16, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=9683655; DOI=10.1007/s002030050629;
RA   Hein S., Tran H., Steinbuechel A.;
RT   "Synechocystis sp. PCC6803 possesses a two-component polyhydroxyalkanoic
RT   acid synthase similar to that of anoxygenic purple sulfur bacteria.";
RL   Arch. Microbiol. 170:162-170(1998).
RN   [3]
RP   SUBCELLULAR LOCATION IN THYLAKOID.
RX   PubMed=16287171; DOI=10.1002/pmic.200500111;
RA   Srivastava R., Pisareva T., Norling B.;
RT   "Proteomic studies of the thylakoid membrane of Synechocystis sp. PCC
RT   6803.";
RL   Proteomics 5:4905-4916(2005).
RN   [4]
RP   FUNCTION, PATHWAY, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, DOMAIN, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=25911471; DOI=10.1128/aem.00604-15;
RA   Hauf W., Watzer B., Roos N., Klotz A., Forchhammer K.;
RT   "Photoautotrophic polyhydroxybutyrate granule formation is regulated by
RT   cyanobacterial phasin PhaP in Synechocystis sp. strain PCC 6803.";
RL   Appl. Environ. Microbiol. 81:4411-4422(2015).
CC   -!- FUNCTION: A phasin, it attaches to the polyhydroxybutyrate (PHB)
CC       granule surface regulating the number and size of PHB granules within a
CC       cell. It probably also acts as a regulator affecting the biosynthetic
CC       activity of PHB synthase in vivo. {ECO:0000269|PubMed:25911471}.
CC   -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC       biosynthesis. {ECO:0000269|PubMed:25911471}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:25911471}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000305|PubMed:16287171}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:16287171}; Cytoplasmic side
CC       {ECO:0000305|PubMed:16287171}. Cytoplasm {ECO:0000269|PubMed:25911471}.
CC       Note=Distributed in cytoplasm during photoautotrophic growth, insoluble
CC       and associated with polyhydroxybutyrate (PHB) granules under nitrogen
CC       starvation (PubMed:25911471, PubMed:9683655).
CC       {ECO:0000269|PubMed:25911471, ECO:0000269|PubMed:9683655}.
CC   -!- INDUCTION: Constitutively expressed, increasing levels as growth
CC       progresses (at protein level). {ECO:0000269|PubMed:25911471}.
CC   -!- DOMAIN: Probably has 2 alpha-helices (resides 3-26 and 39-83); both
CC       helices alone target to PHB granules, although helix 2 may be the main
CC       anchor. Both helices are required for oligomerization.
CC       {ECO:0000269|PubMed:25911471}.
CC   -!- DISRUPTION PHENOTYPE: During N(2) starvation fewer PHB granules
CC       accumulate per cell, while their diameter is increased by about 25%
CC       after 6 days of nitrogen starvation. Decreased rate of PHB synthesis,
CC       however overall accumulation of PHB is not significantly different.
CC       {ECO:0000269|PubMed:25911471}.
CC   -!- BIOTECHNOLOGY: Poly(3-hydroxyalkanoic acids) (PHA), of which PHB is
CC       among the most common compounds, are prokaryotic intracellular storage
CC       compounds with potential uses as a renewable, biodegradable
CC       thermoplastic. Cyanobacterial PHB synthesis is particularly attractive
CC       as cyanobacteria use CO(2) as the carbon source. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Nitrogen-free medium induces chlorosis in Synechocystis,
CC       leading to the degradation of the photosynthetic apparatus and
CC       concomitant accumulation of cytoplasmic polyhydroxyalkanoic acid (PHA)
CC       granules which in this cyanobacterium are composed of PHB.
CC       {ECO:0000305|PubMed:25911471}.
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DR   EMBL; BA000022; BAA17585.1; -; Genomic_DNA.
DR   PIR; S77251; S77251.
DR   AlphaFoldDB; P73545; -.
DR   SMR; P73545; -.
DR   STRING; 1148.1652665; -.
DR   PaxDb; P73545; -.
DR   EnsemblBacteria; BAA17585; BAA17585; BAA17585.
DR   KEGG; syn:ssl2501; -.
DR   eggNOG; ENOG5032ZT5; Bacteria.
DR   OMA; KFFDTWL; -.
DR   UniPathway; UPA00917; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0070088; C:PHA granule; IDA:UniProtKB.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Membrane; PHB biosynthesis;
KW   Reference proteome; Thylakoid.
FT   CHAIN           1..89
FT                   /note="Phasin PhaP"
FT                   /id="PRO_0000352746"
FT   REGION          3..26
FT                   /note="Helix 1"
FT                   /evidence="ECO:0000305|PubMed:25911471"
FT   REGION          39..83
FT                   /note="Helix 2"
FT                   /evidence="ECO:0000305|PubMed:25911471"
SQ   SEQUENCE   89 AA;  10648 MW;  7AB8755B0C7DB97A CRC64;
     MNTQFFEEYQ TQLLDWQKKF FSTWMESLPK GTAEIKLTDT FETSLKLQEE MVKSYLEAQE
     KSATMMIDAQ KQFWDNYFQA LRQEPVSAN
 
 
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