GLPC_ECO57
ID GLPC_ECO57 Reviewed; 396 AA.
AC P0A997; P13034; P76927; P77679;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit C;
DE Short=G-3-P dehydrogenase;
GN Name=glpC; OrderedLocusNames=Z3501, ECs3128;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Electron transfer protein; may also function as the membrane
CC anchor for the GlpAB dimer. {ECO:0000250}.
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC route): step 1/1.
CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of GlpC.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC Note=Loosely bound to the cytoplasmic membrane often occurring in
CC vesicles associated with fumarate reductase. {ECO:0000250}.
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DR EMBL; AE005174; AAG57374.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36551.1; -; Genomic_DNA.
DR PIR; B85864; B85864.
DR PIR; H91019; H91019.
DR RefSeq; NP_311155.1; NC_002695.1.
DR RefSeq; WP_001000379.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A997; -.
DR STRING; 155864.EDL933_3407; -.
DR PRIDE; P0A997; -.
DR EnsemblBacteria; AAG57374; AAG57374; Z3501.
DR EnsemblBacteria; BAB36551; BAB36551; ECs_3128.
DR GeneID; 916836; -.
DR KEGG; ece:Z3501; -.
DR KEGG; ecs:ECs_3128; -.
DR PATRIC; fig|386585.9.peg.3262; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_7_1_6; -.
DR OMA; FQRCCGA; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1060.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR017753; G3P_DH_GlpC_su.
DR InterPro; IPR009051; Helical_ferredxn.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13183; Fer4_8; 1.
DR TIGRFAMs; TIGR03379; glycerol3P_GlpC; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..396
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT C"
FT /id="PRO_0000159260"
FT DOMAIN 2..29
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 45..76
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 9
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 44108 MW; 1DC9203332B6F2F2 CRC64;
MNDTSFENCI KCTVCTTACP VSRVNPGYPG PKQAGPDGER LRLKDGALYD EALKYCINCK
RCEVACPSDV KIGDIIQRAR AKYDTTRPSL RNFVLSHTDL MGSVSTPFAP IVNTATSLKP
VRQLLDAALK IDHRRTLPKY SFGTFRRWYR SVAAQQAQYK DQVAFFHGCF VNYNHPQLGK
DLIKVLNAMG TGVQLLSKEK CCGVPLIANG FTDKARKQAI TNVESIREAV GVKGIPVIAT
SSTCTFALRD EYPEVLNVDN KGLRDHIELA TRWLWRKLDE GKTLPLKPLP LKVVYHTPCH
MEKMGWTLYT LELLRNIPGL ELTVLDSQCC GIAGTYGFKK ENYPTSQAIG APLFRQIEES
GADLVVTDCE TCKWQIEMST SLRCEHPITL LAQALA
