PSAB_GLOVI
ID PSAB_GLOVI Reviewed; 872 AA.
AC Q7NFT5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2;
DE EC=1.97.1.12;
DE AltName: Full=PsaB;
GN Name=psaB; OrderedLocusNames=glr3439;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CHARACTERIZATION OF PHOTOSYSTEM I.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=15589832; DOI=10.1016/j.febslet.2004.11.013;
RA Inoue H., Tsuchiya T., Satoh S., Miyashita H., Kaneko T., Tabata S.,
RA Tanaka A., Mimuro M.;
RT "Unique constitution of photosystem I with a novel subunit in the
RT cyanobacterium Gloeobacter violaceus PCC 7421.";
RL FEBS Lett. 578:275-279(2004).
CC -!- FUNCTION: PsaA and PsaB bind P700, the primary electron donor of
CC photosystem I (PSI), as well as the electron acceptors A0, A1 and FX.
CC PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase,
CC converting photonic excitation into a charge separation, which
CC transfers an electron from the donor P700 chlorophyll pair to the
CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in
CC turn. Oxidized P700 is reduced on the lumenal side of the thylakoid
CC membrane by plastocyanin or cytochrome c6.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin]
CC = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036,
CC ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:49552; EC=1.97.1.12;
CC -!- COFACTOR:
CC Note=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2
CC phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll
CC a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a
CC chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1
CC is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur
CC center. {ECO:0000250};
CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special pair
CC and subsequent electron acceptors. PSI consists of a core antenna
CC complex that captures photons, and an electron transfer chain that
CC converts photonic excitation into a charge separation. The G.violaceus
CC PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,L,M
CC and Z, and forms trimeric complexes.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: The C-terminal extension has been suggested to be able
CC to bind to the peptidoglycan layer. {ECO:0000305|PubMed:15589832}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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DR EMBL; BA000045; BAC91380.1; -; Genomic_DNA.
DR RefSeq; NP_926385.1; NC_005125.1.
DR RefSeq; WP_011143428.1; NC_005125.1.
DR PDB; 7F4V; EM; 2.04 A; aB/bB/cB=1-872.
DR PDBsum; 7F4V; -.
DR AlphaFoldDB; Q7NFT5; -.
DR SMR; Q7NFT5; -.
DR STRING; 251221.35214011; -.
DR EnsemblBacteria; BAC91380; BAC91380; BAC91380.
DR KEGG; gvi:glr3439; -.
DR PATRIC; fig|251221.4.peg.3471; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR InParanoid; Q7NFT5; -.
DR OMA; FEQWVAD; -.
DR OrthoDB; 36958at2; -.
DR PhylomeDB; Q7NFT5; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 1.20.1130.10; -; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR001280; PSI_PsaA/B.
DR InterPro; IPR020586; PSI_PsaA/B_CS.
DR InterPro; IPR036408; PSI_PsaA/B_sf.
DR InterPro; IPR006244; PSI_PsaB.
DR Pfam; PF00691; OmpA; 1.
DR Pfam; PF00223; PsaA_PsaB; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF103088; SSF103088; 1.
DR SUPFAM; SSF81558; SSF81558; 1.
DR TIGRFAMs; TIGR01336; psaB; 1.
DR PROSITE; PS51123; OMPA_2; 1.
DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell inner membrane; Cell membrane; Chlorophyll;
KW Chromophore; Electron transport; Iron; Iron-sulfur; Magnesium; Membrane;
KW Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..872
FT /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT /id="PRO_0000088644"
FT TRANSMEM 46..69
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..158
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..199
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..279
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..339
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..381
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..425
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..517
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..578
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..648
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255"
FT TRANSMEM 690..710
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255"
FT DOMAIN 745..868
FT /note="OmpA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00473"
FT REGION 1..717
FT /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT REGION 829..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 541
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 550
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 637
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 645
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 653
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /evidence="ECO:0000250"
FT BINDING 654
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
SQ SEQUENCE 872 AA; 96073 MW; 8576DE66B6670C8C CRC64;
MATRFPKFSQ DLAQDPTTRR IWYGIATAHD FESHDGMTEE SLYQKLFATH FGHLAIIFLW
SSGNLFHIAW QGNFEQWVSN PTGVVPIAHA IWDPHFGKGA VEAFTPEGGA GPVNAAYSGL
YYLYYTLGMR FNSDLYQGSI FLMVLATVFL IAGWLHLQPR FRPSLAWFKN AESRLNHHLS
ALFGVSSLAF AGHMIHVAIP AARGQRVDWS NFLNTLPHPA GLAPFFTGNW GVYADPQAGP
PILTFIGGLN PATGTLWLTD IAHHHLAIAV IFIIAGHMYR TNFGIGHSIK EILDAHKGPL
TGEGHRGLYD TINNSLHFQL GLALASLGVV TSLVAQHTYA LPAYFYMPQD HTTMAALYTH
HQYIAGFLMV GAFAHGAIFF VRDYDPKANE NNVLARMLEH KEALISHLSW VSLFLGFHTL
GLYVHNDVML AFGRPEDQLL IEPVFAQFVQ VQSGKIIEGI PALFGGPGVT APGEFLTGWL
GSVNANNSPI FLPIGPGDFL VHHAIALGLH TTTLILVKGA LDARGSKLMP DKKDFGFAFP
CDGPGRGGTC DISAWDAFYL AVFWMLNTIG WVTFYWHWKW ISIWGDNVAQ FNASSTYLMG
WLRDYLWANS APLIGGYSPS GGTNALSVWA WMFLFGHLVW ATGFMFLIAW RGYWQELIET
LVWAHERTPL ANLVRWKDKP VAMSIVQGRL VGLAHFTIGY ILTYAAFLIA STAALYPNGP
AAFTPAISAE QAKGVLSEFK AKPVPGGVML LLPENIVFDF DKSSVKLDAD PALNRVVGVI
QFYGSEPVEI LGHTDSLGED AYNQKLSEER ASAVKAFFEK KGIEAERLTA KGYGETKPVA
PNAKPDGSDN PDGRQQNRRV EILIKTEVVP VS
