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Database: UniProt
Entry: A0A0M2PXM2_PROHO
LinkDB: A0A0M2PXM2_PROHO
Original site: A0A0M2PXM2_PROHO 
ID   A0A0M2PXM2_PROHO        Unreviewed;       163 AA.
AC   A0A0M2PXM2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   18-JUN-2025, entry version 35.
DE   RecName: Full=Photosystem II extrinsic protein V {ECO:0000256|HAMAP-Rule:MF_01378};
DE            Short=PsbV {ECO:0000256|HAMAP-Rule:MF_01378};
DE   AltName: Full=Cytochrome c-550 {ECO:0000256|HAMAP-Rule:MF_01378};
DE   AltName: Full=Cytochrome c550 {ECO:0000256|HAMAP-Rule:MF_01378};
DE   AltName: Full=Low-potential cytochrome c {ECO:0000256|HAMAP-Rule:MF_01378};
DE   Flags: Precursor;
GN   Name=psbV {ECO:0000256|HAMAP-Rule:MF_01378,
GN   ECO:0000313|EMBL:KKI99418.1};
GN   ORFNames=PROH_16470 {ECO:0000313|EMBL:KKI99418.1};
OS   Prochlorothrix hollandica PCC 9006 = CALU 1027.
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Prochlorotrichales;
OC   Prochlorotrichaceae; Prochlorothrix.
OX   NCBI_TaxID=317619 {ECO:0000313|EMBL:KKI99418.1, ECO:0000313|Proteomes:UP000034681};
RN   [1] {ECO:0000313|EMBL:KKI99418.1, ECO:0000313|Proteomes:UP000034681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CALU 1027 {ECO:0000313|EMBL:KKI99418.1};
RA   Shanker A., Yadav P., Khan S., Sharma V.;
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKI99418.1, ECO:0000313|Proteomes:UP000034681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CALU 1027 {ECO:0000313|EMBL:KKI99418.1};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the extrinsic, lumenal subunits of photosystem II
CC       (PSII). PSII is a light-driven water plastoquinone oxidoreductase,
CC       using light energy to abstract electrons from H(2)O, generating a
CC       proton gradient subsequently used for ATP formation. The extrinsic
CC       proteins stabilize the structure of photosystem II oxygen-evolving
CC       complex (OEC), the ion environment of oxygen evolution and protect the
CC       OEC against heat-induced inactivation. Low-potential cytochrome c that
CC       plays a role in the OEC of PSII. {ECO:0000256|HAMAP-Rule:MF_01378}.
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01378};
CC       Note=Binds 1 heme c group covalently per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01378};
CC   -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC       PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC       PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ),
CC       PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000256|HAMAP-Rule:MF_01378}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01378}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01378}; Lumenal side {ECO:0000256|HAMAP-Rule:MF_01378}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Note=Associated with photosystem II at
CC       the lumenal side of the thylakoid membrane. {ECO:0000256|HAMAP-
CC       Rule:MF_01378}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily.
CC       {ECO:0000256|ARBA:ARBA00010433, ECO:0000256|HAMAP-Rule:MF_01378}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKI99418.1}.
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DR   EMBL; AJTX02000006; KKI99418.1; -; Genomic_DNA.
DR   RefSeq; WP_026099567.1; NZ_KB235937.1.
DR   AlphaFoldDB; A0A0M2PXM2; -.
DR   STRING; 317619.GCA_000332315_02476; -.
DR   eggNOG; COG2010; Bacteria.
DR   OrthoDB; 486949at2; -.
DR   Proteomes; UP000034681; Unassembled WGS sequence.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   HAMAP; MF_01378; PSII_Cyt550; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR029490; Cytochrom_C550.
DR   InterPro; IPR017851; PsbV_cyt_c550.
DR   InterPro; IPR016003; PsbV_cyt_c550-like.
DR   NCBIfam; TIGR03045; PS_II_C550; 1.
DR   Pfam; PF14495; Cytochrom_C550; 1.
DR   PIRSF; PIRSF005890; Phot_II_cyt_c550; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_01378};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01378};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01378};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01378};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01378};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_01378};
KW   Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW   Rule:MF_01378}; Reference proteome {ECO:0000313|Proteomes:UP000034681};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_01378};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01378};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01378}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   CHAIN           27..163
FT                   /note="Photosystem II extrinsic protein V"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT                   /id="PRO_5008991652"
FT   DOMAIN          50..149
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         63
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   BINDING         66
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   BINDING         67
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   BINDING         118
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
SQ   SEQUENCE   163 AA;  17623 MW;  689EE7B5DF9D6EA9 CRC64;
     MMKKSFLLSL AALLMAFGFL GGSAWAASLD KETLTIPLNA MGDTTVLSVE QVIQGERLFN
     DKCAVCHNSG GTKTNPNVGL GADDLSFAVP ARNNLEGMVD YLNNPTSYDG EYSIALFHPS
     IKSAVVFPKM RDVDQDDLKA ISGYVLIQPK VQPDRWGAGK YAF
//
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