ID Q79EF9_SYNY3 Unreviewed; 330 AA. AC Q79EF9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 129. DE SubName: Full=Mn transporter MntC {ECO:0000313|EMBL:BAA17919.1}; GN Name=mntC {ECO:0000313|EMBL:BAA17919.1}; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA17919.1, ECO:0000313|Proteomes:UP000001425}; RN [1] {ECO:0000313|EMBL:BAA17919.1, ECO:0000313|Proteomes:UP000001425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425}; 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] {ECO:0007829|PDB:1XVL} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 26-330 IN COMPLEX WITH MANGANESE, RP AND DISULFIDE BONDS. RX PubMed=15843026; DOI=10.1016/j.jmb.2005.03.006; RA Rukhman V., Anati R., Melamed-Frank M., Adir N.; RT "The MntC crystal structure suggests that import of Mn2+ in cyanobacteria RT is redox controlled."; RL J. Mol. Biol. 348:961-969(2005). RN [3] {ECO:0007829|PDB:3UJP, ECO:0007829|PDB:4IRM} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 24-330 IN COMPLEX WITH MANGANESE RP AND ZINC, AND DISULFIDE BONDS. RX PubMed=23519795; DOI=10.1107/S174430911300153X; RA Kanteev M., Adir N.; RT "Arginine 116 stabilizes the entrance to the metal ion-binding site of the RT MntC protein."; RL Acta Crystallogr. F Struct. Biol. Commun. 69:237-242(2013). CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family. CC {ECO:0000256|RuleBase:RU003512}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000022; BAA17919.1; -; Genomic_DNA. DR PDB; 1XVL; X-ray; 2.90 A; A/B/C=26-330. DR PDB; 3UJP; X-ray; 2.70 A; A/B/C=24-330. DR PDB; 4IRM; X-ray; 3.50 A; A/B/C=1-330. DR PDBsum; 1XVL; -. DR PDBsum; 3UJP; -. DR PDBsum; 4IRM; -. DR AlphaFoldDB; Q79EF9; -. DR SMR; Q79EF9; -. DR IntAct; Q79EF9; 1. DR STRING; 1148.gene:10498788; -. DR PaxDb; 1148-1653002; -. DR EnsemblBacteria; BAA17919; BAA17919; BAA17919. DR KEGG; syn:sll1598; -. DR eggNOG; COG0803; Bacteria. DR InParanoid; Q79EF9; -. DR PhylomeDB; Q79EF9; -. DR EvolutionaryTrace; Q79EF9; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR CDD; cd01137; PsaA; 1. DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2. DR InterPro; IPR006129; AdhesinB. DR InterPro; IPR006128; Lipoprotein_PsaA-like. DR InterPro; IPR006127; ZnuA-like. DR PANTHER; PTHR42953; HIGH-AFFINITY ZINC UPTAKE SYSTEM PROTEIN ZNUA-RELATED; 1. DR PANTHER; PTHR42953:SF1; MANGANESE ABC TRANSPORTER SUBSTRATE-BINDING LIPOPROTEIN; 1. DR Pfam; PF01297; ZnuA; 1. DR PRINTS; PR00691; ADHESINB. DR PRINTS; PR00690; ADHESNFAMILY. DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1XVL, ECO:0007829|PDB:3UJP}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:1XVL}; KW Reference proteome {ECO:0000313|Proteomes:UP000001425}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003512}; KW Zinc {ECO:0007829|PDB:3UJP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..330 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004287721" FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3UJP" FT BINDING 74 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3UJP" FT BINDING 89 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:1XVL, ECO:0007829|PDB:3UJP" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3UJP" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3UJP" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:3UJP" FT BINDING 127 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:3UJP" FT BINDING 135 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0007829|PDB:3UJP" FT BINDING 138 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3UJP" FT BINDING 154 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:1XVL, ECO:0007829|PDB:3UJP" FT BINDING 207 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:3UJP" FT BINDING 220 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:1XVL, ECO:0007829|PDB:3UJP" FT BINDING 295 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:1XVL, ECO:0007829|PDB:3UJP" FT BINDING 300 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:3UJP" FT DISULFID 219..268 FT /evidence="ECO:0007829|PDB:1XVL, ECO:0007829|PDB:3UJP" SQ SEQUENCE 330 AA; 36075 MW; FE9F510020719D80 CRC64; MATSFASRGG LLASGLAIAF WLTGCGTAEV TTSNAPSEEV TAVTTEVQGE TEEKKKVLTT FTVLADMVQN VAGDKLVVES ITRIGAEIHG YEPTPSDIVK AQDADLILYN GMNLERWFEQ FLGNVKDVPS VVLTEGIEPI PIADGPYTDK PNPHAWMSPR NALVYVENIR QAFVELDPDN AKYYNANAAV YSEQLKAIDR QLGADLEQVP ANQRFLVSCE GAFSYLARDY GMEEIYMWPI NAEQQFTPKQ VQTVIEEVKT NNVPTIFCES TVSDKGQKQV AQATGARFGG NLYVDSLSTE EGPVPTFLDL LEYDARVITN GLLAGTNAQQ //