YCF48_SYNY3
ID YCF48_SYNY3 Reviewed; 342 AA.
AC P73069;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Photosystem II assembly lipoprotein Ycf48 {ECO:0000255|HAMAP-Rule:MF_01348, ECO:0000303|PubMed:33918522};
DE Flags: Precursor;
GN Name=ycf48 {ECO:0000255|HAMAP-Rule:MF_01348, ECO:0000303|PubMed:8905231};
GN OrderedLocusNames=slr2034;
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 34-47; 52-76; 83-219; 222-253 AND 260-339, SUBCELLULAR
RP LOCATION, PROBABLE PALMITOYLATION AT CYS-29, PROBABLE DIACYLGLYCEROL AT
RP CYS-29, C-TERMINAL PROCESSING, MASS SPECTROMETRY, AND MUTAGENESIS OF
RP 26-CYS--CYS-29; CYS-26 AND CYS-29.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=33918522; DOI=10.3390/ijms22073733;
RA Knoppova J., Yu J., Janouskovec J., Halada P., Nixon P.J., Whitelegge J.P.,
RA Komenda J.;
RT "The Photosystem II Assembly Factor Ycf48 from the Cyanobacterium
RT Synechocystis sp. PCC 6803 Is Lipidated Using an Atypical Lipobox
RT Sequence.";
RL Int. J. Mol. Sci. 22:0-0(2021).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=18550538; DOI=10.1074/jbc.m801917200;
RA Komenda J., Nickelsen J., Tichy M., Prasil O., Eichacker L.A., Nixon P.J.;
RT "The cyanobacterial homologue of HCF136/YCF48 is a component of an early
RT photosystem II assembly complex and is important for both the efficient
RT assembly and repair of photosystem II in Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 283:22390-22399(2008).
RN [4]
RP FUNCTION, INTERACTION WITH YIDC, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-176; 196-ARG--ARG-219;
RP 196-ARG--ARG-220; ARG-196; 215-ARG--ARG-220; ARG-215; ARG-219 AND ARG-220.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=30061392; DOI=10.1073/pnas.1800609115;
RA Yu J., Knoppova J., Michoux F., Bialek W., Cota E., Shukla M.K.,
RA Straskova A., Pascual Aznar G., Sobotka R., Komenda J., Murray J.W.,
RA Nixon P.J.;
RT "Ycf48 involved in the biogenesis of the oxygen-evolving photosystem II
RT complex is a seven-bladed beta-propeller protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E7824-E7833(2018).
CC -!- FUNCTION: A factor required for optimal assembly of photosystem II
CC (PSII) which acts in the early stages of PSII assembly. Also plays a
CC role in replacement of photodamaged D1 (psbA) (PubMed:18550538). May
CC interact with precursor D1 to prevent its premature processing before
CC association with D2 (psbD) (PubMed:18550538) (Probable). May also play
CC a role in chlorophyll insertion into chlorophyll-binding proteins
CC (PubMed:18550538) (Probable). Increasing levels of chlorophyll
CC precursors partially suppresses deletion of this protein, supporting
CC the idea that Ycf48 assists YidC in synthesis of chlorophyll-binding
CC proteins (PubMed:30061392). {ECO:0000269|PubMed:18550538,
CC ECO:0000269|PubMed:30061392, ECO:0000305|PubMed:18550538}.
CC -!- SUBUNIT: Part of early PSII assembly complexes which includes D1 (psbA)
CC and PsbI; not found in mature PSII. By two-hybrid analysis in yeast
CC interacts with precursor and intermediate forms of D1, but less with
CC mature D1 (PubMed:18550538). Binds to the lumenal side of PSI and PSII
CC complexes. Coimmunoprecipitates with YidC (PubMed:30061392).
CC {ECO:0000269|PubMed:18550538, ECO:0000269|PubMed:30061392}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01348, ECO:0000269|PubMed:18550538,
CC ECO:0000269|PubMed:33918522}; Lipid-anchor
CC {ECO:0000269|PubMed:33918522}; Lumenal side
CC {ECO:0000269|PubMed:30061392}. Note=Associated with a PSII precusor
CC complex on the lumenal side of the thylakoid membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01348, ECO:0000269|PubMed:30061392}.
CC -!- DOMAIN: Eukaryotic orthologs often have inserts compared to
CC cyanobacteria; insertion of a 19-residue sequence from C.merolae into
CC the same position in this protein (at Val-176) has no visible effect on
CC function. An Arg-rich patch composed of 4 residues on the 'top surface'
CC of blades 4 and 5 is important for binding to assembling PSII centers;
CC mutating each Arg residue individually has no phenotype whereas none of
CC the triple mutants grow in high light (90-130 umol photon/m(2)/s),
CC suggesting more than one residue is involved in binding to the lumenal
CC side of assembling PSII centers. {ECO:0000269|PubMed:30061392}.
CC -!- DOMAIN: A 7-bladed beta-propeller torus, about 55 by 55 Angstroms, with
CC a depth of about 25 Angstroms and a central pore. {ECO:0000255|HAMAP-
CC Rule:MF_01348}.
CC -!- PTM: The last 3 residues are removed in the mature protein.
CC {ECO:0000269|PubMed:33918522}.
CC -!- MASS SPECTROMETRY: Mass=33689.1; Method=MALDI; Note=Modified with
CC diacylglycerol and acylation on Cys-29, with last 3 residues removed.;
CC Evidence={ECO:0000269|PubMed:33918522};
CC -!- MASS SPECTROMETRY: Mass=33428.1; Method=MALDI; Note=Single fatty acid
CC on Cys-29, with last 3 residues removed.;
CC Evidence={ECO:0000269|PubMed:33918522};
CC -!- DISRUPTION PHENOTYPE: Grows significantly slower than wild-type, 30-50%
CC reduction in functional PSII, decreased chlorophyll content,
CC significantly reduced replacement of photodamaged D1 (psbA)
CC (PubMed:18550538). Grows poorly on low light (40-50 umol photon/m(2)/s)
CC and not on higher light, reduced chlorophyll, increased levels of
CC unassembled D1, substantially reduced levels of chlorophyll precursors
CC (PubMed:30061392). {ECO:0000269|PubMed:18550538,
CC ECO:0000269|PubMed:30061392}.
CC -!- SIMILARITY: Belongs to the Ycf48 family. {ECO:0000255|HAMAP-
CC Rule:MF_01348}.
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DR EMBL; BA000022; BAA17091.1; -; Genomic_DNA.
DR PIR; S75177; S75177.
DR AlphaFoldDB; P73069; -.
DR SMR; P73069; -.
DR IntAct; P73069; 4.
DR STRING; 1148.1652167; -.
DR PaxDb; P73069; -.
DR EnsemblBacteria; BAA17091; BAA17091; BAA17091.
DR KEGG; syn:slr2034; -.
DR eggNOG; COG4447; Bacteria.
DR InParanoid; P73069; -.
DR OMA; EGWIAGQ; -.
DR PhylomeDB; P73069; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0010207; P:photosystem II assembly; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR HAMAP; MF_01348; Ycf48; 1.
DR InterPro; IPR028203; PSII_CF48-like_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR016705; Ycf48/Hcf136.
DR Pfam; PF14870; PSII_BNR; 1.
DR PIRSF; PIRSF017875; PSII_HCF136; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Photosynthesis; Photosystem II; Reference proteome; Signal; Thylakoid.
FT SIGNAL 1..28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01348"
FT CHAIN 29..339
FT /note="Photosystem II assembly lipoprotein Ycf48"
FT /evidence="ECO:0000269|PubMed:33918522"
FT /id="PRO_0000217373"
FT PROPEP 340..342
FT /evidence="ECO:0000269|PubMed:33918522"
FT /id="PRO_0000456141"
FT MOTIF 196..220
FT /note="Arg-rich patch"
FT /evidence="ECO:0000269|PubMed:30061392"
FT LIPID 29
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:33918522"
FT LIPID 29
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:33918522"
FT MUTAGEN 26..29
FT /note="CVSC->AVSA: Almost complete loss of thylakoid
FT targeting, normal autotrophic and photoheterotrophic
FT growth."
FT /evidence="ECO:0000269|PubMed:33918522"
FT MUTAGEN 26
FT /note="C->A: No change in thylakoid targeting, normal
FT autotrophic and photoheterotrophic growth."
FT /evidence="ECO:0000269|PubMed:33918522"
FT MUTAGEN 29
FT /note="C->A: Almost complete loss of thylakoid targeting,
FT normal autotrophic and photoheterotrophic growth."
FT /evidence="ECO:0000269|PubMed:33918522"
FT MUTAGEN 176
FT /note="V->VDATLNRTISSGITGASYFTG: Behaves like wild-type,
FT has insert of C.merolae."
FT /evidence="ECO:0000269|PubMed:30061392"
FT MUTAGEN 196..220
FT /note="RGNFYSTWAPGQTEWTPHNRNSSRR->AGNFYSTWAPGQTEWTPHNANSSAA
FT : Not as extreme effect as mutating same residues to E,
FT unable to grow in high light (90-130 umol photon/m(2)/s),
FT replaces Arg-patch with Ala."
FT /evidence="ECO:0000269|PubMed:30061392"
FT MUTAGEN 196..220
FT /note="RGNFYSTWAPGQTEWTPHNRNSSRR->EGNFYSTWAPGQTEWTPHNENSSEE
FT : Decreased chlorophyll content, unable to grow in medium
FT light (70-90 umol photon/m(2)/s), impaired assembly of PS
FT complexes, does not bind PSI or PSII, replaces Arg-patch
FT with Glu."
FT /evidence="ECO:0000269|PubMed:30061392"
FT MUTAGEN 196..219
FT /note="RGNFYSTWAPGQTEWTPHNRNSSR->EGNFYSTWAPGQTEWTPHNENSSE:
FT Grows very poorly in medium light (70-90 umol
FT photon/m(2)/(s)), replaces first 3 residues of Arg-patch."
FT /evidence="ECO:0000269|PubMed:30061392"
FT MUTAGEN 196
FT /note="R->E: No visible phenotype."
FT /evidence="ECO:0000269|PubMed:30061392"
FT MUTAGEN 215..220
FT /note="RNSSRR->ENSEE: Grows very poorly in medium light
FT (70-90 umol photon/m(2)/(s)), replaces last 3 residues of
FT Arg-patch."
FT /evidence="ECO:0000269|PubMed:30061392"
FT MUTAGEN 215
FT /note="R->E: No visible phenotype."
FT /evidence="ECO:0000269|PubMed:30061392"
FT MUTAGEN 219
FT /note="R->E: No visible phenotype."
FT /evidence="ECO:0000269|PubMed:30061392"
FT MUTAGEN 220
FT /note="R->E: No visible phenotype."
FT /evidence="ECO:0000269|PubMed:30061392"
SQ SEQUENCE 342 AA; 37291 MW; 9AB2A72B82DA046A CRC64;
MPVKFPSLKF EQLKQLVLVA AIAVFCVSCS HVPDLAFNPW QEIALETDST FADIAFTEDP
NHGWLVGTKE TIFETTDGGD TWEQKLIDLG EEKASFSAVS FSGNEGWITG KPSILLHTTD
GGQTWARIPL SEKLPGAPYS IIALGPQTAE MITDLGAIYK TTNGGKNWKA LVEGAVGVAR
TIQRSTDGRY VAVSARGNFY STWAPGQTEW TPHNRNSSRR LQTMGYGKDG QLWLLARGGQ
LQFSTDPDAE EWSDVIAPQD KGSWGLLDLS FRTPEEVWVA GASGNLLMSQ DGGQTWAKDT
GVEDIPANLY RVVFLSPEKG FVLGQDGILL KYNPSTEVAM VP
