ID Q8NTB8_CORGL Unreviewed; 359 AA.
AC Q8NTB8; Q6M7X3;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE SubName: Full=ABC-type transporter, periplasmic component {ECO:0000313|EMBL:BAB97782.1};
GN OrderedLocusNames=Cgl0389 {ECO:0000313|EMBL:BAB97782.1};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB97782.1, ECO:0000313|Proteomes:UP000000582};
RN [1] {ECO:0000313|Proteomes:UP000000582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC NCIMB 10025 {ECO:0000313|Proteomes:UP000000582};
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2] {ECO:0007829|PDB:5AZ3}
RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 24-359 IN COMPLEX WITH HEME B.
RX DOI=10.1246/cl.150894;
RA Muraki N., Aono S.;
RT "Structural Basis for Heme Recognition by HmuT Responsible for Heme
RT Transport to the Heme Transporter in Corynebacterium glutamicum.";
RL Chem. Lett. 0:0-0(2015).
RN [3] {ECO:0007829|PDB:5B4Z, ECO:0007829|PDB:5B50}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 24-359 IN COMPLEX WITH HEME B.
RX PubMed=27240352; DOI=10.3390/ijms17060829;
RA Muraki N., Kitatsuji C., Ogura M., Uchida T., Ishimori K., Aono S.;
RT "Structural Characterization of Heme Environmental Mutants of CgHmuT that
RT Shuttles Heme Molecules to Heme Transporters. .";
RL Int. J. Mol. Sci. 17:E829-E829(2016).
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DR EMBL; BA000036; BAB97782.1; -; Genomic_DNA.
DR RefSeq; NP_599637.1; NC_003450.3.
DR RefSeq; WP_003859750.1; NC_006958.1.
DR PDB; 5AZ3; X-ray; 1.42 A; A=24-359.
DR PDB; 5B4Z; X-ray; 1.30 A; A=24-359.
DR PDB; 5B50; X-ray; 1.65 A; A=24-359.
DR PDB; 5B51; X-ray; 1.30 A; A=24-359.
DR PDBsum; 5AZ3; -.
DR PDBsum; 5B4Z; -.
DR PDBsum; 5B50; -.
DR PDBsum; 5B51; -.
DR AlphaFoldDB; Q8NTB8; -.
DR SMR; Q8NTB8; -.
DR STRING; 196627.cg0467; -.
DR DNASU; 1021159; -.
DR KEGG; cgl:Cgl0389; -.
DR PATRIC; fig|196627.13.peg.390; -.
DR eggNOG; COG4558; Bacteria.
DR HOGENOM; CLU_038034_6_1_11; -.
DR OrthoDB; 9797736at2; -.
DR BioCyc; CORYNE:G18NG-9946-MONOMER; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR PANTHER; PTHR30535:SF4; HEMIN-BINDING PERIPLASMIC PROTEIN HMUT; 1.
DR PANTHER; PTHR30535; VITAMIN B12-BINDING PROTEIN; 1.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR PROSITE; PS50983; FE_B12_PBP; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5AZ3, ECO:0007829|PDB:5B4Z};
KW Heme {ECO:0007829|PDB:5AZ3, ECO:0007829|PDB:5B4Z};
KW Iron {ECO:0007829|PDB:5AZ3, ECO:0007829|PDB:5B4Z};
KW Metal-binding {ECO:0007829|PDB:5AZ3, ECO:0007829|PDB:5B4Z};
KW Reference proteome {ECO:0000313|Proteomes:UP000000582};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..359
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004313109"
FT DOMAIN 97..359
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000259|PROSITE:PS50983"
FT BINDING 141
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:5B50"
FT BINDING 141
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:5AZ3, ECO:0007829|PDB:5B51"
FT BINDING 240
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:5AZ3, ECO:0007829|PDB:5B51"
FT BINDING 240
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:5B4Z"
SQ SEQUENCE 359 AA; 37330 MW; 60C13202D749E32A CRC64;
MNNAFRRTLT SVVLAASLAL TACASWDSPT ASSNGDLIEE IQASSTSTDP RTFTGLSIVE
DIGDVVPVTD NASPALPVSL TDADGNDVVV EDVSRILPLD LYGTYSKTIA GLGLVDNIVG
RTVSSTEPAL ADTEVVTTGG HTLNAEAILN LHPTLVIIDH SIGPREVIDQ IRAAGVATVI
MSPQRSIASI GDDIRDIASV VGLPEEGEKL AERSVAEVEE ASTVVDELTP EDPLKMVFLY
ARGTGGVFFI LGDAYGGRDL IEGLGGVDMA AEKGIMDLAP ANAEALAELN PDVFVMMSEG
LVSTGGIDGL MERPGIAQTT AGQNQRVLAL PDGQSLAFGA QTGELLLRAS RELYVQGGE
//
