PHSC_SALTY
ID PHSC_SALTY Reviewed; 254 AA.
AC P37602; P37603; Q56120;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Thiosulfate reductase cytochrome B subunit PhsC {ECO:0000305};
DE AltName: Full=Thiosulfate reductase subunit gamma {ECO:0000305};
GN Name=phsC {ECO:0000303|PubMed:7751291}; OrderedLocusNames=STM2063;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7751291; DOI=10.1128/jb.177.10.2813-2820.1995;
RA Heinzinger N.K., Fujimoto S.Y., Clark M.A., Moreno M.S., Barrett E.L.;
RT "Sequence analysis of the phs operon in Salmonella typhimurium and the
RT contribution of thiosulfate reduction to anaerobic energy metabolism.";
RL J. Bacteriol. 177:2813-2820(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7737516; DOI=10.1016/0378-1119(94)00930-q;
RA Alami N., Hallenbeck P.C.;
RT "Cloning and characterization of a gene cluster, phsBCDEF, necessary for
RT the production of hydrogen sulfide from thiosulfate by Salmonella
RT typhimurium.";
RL Gene 156:53-57(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP FUNCTION.
RC STRAIN=LT2;
RX PubMed=3108233; DOI=10.1128/jb.169.6.2391-2397.1987;
RA Clark M.A., Barrett E.L.;
RT "The phs gene and hydrogen sulfide production by Salmonella typhimurium.";
RL J. Bacteriol. 169:2391-2397(1987).
RN [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=22081391; DOI=10.1128/jb.06014-11;
RA Stoffels L., Krehenbrink M., Berks B.C., Unden G.;
RT "Thiosulfate reduction in Salmonella enterica is driven by the proton
RT motive force.";
RL J. Bacteriol. 194:475-485(2012).
CC -!- FUNCTION: Component of the PhsABC thiosulfate reductase that catalyzes
CC the reduction of thiosulfate to sulfite and hydrogen sulfide, with
CC menaquinol as the sole electron donor. Proton motive force (PMF) is
CC required to drive transmembrane electron transfer within the reductase.
CC The PhsC subunit anchors the complex to the membrane and contains the
CC site for menaquinol oxidation. {ECO:0000269|PubMed:22081391,
CC ECO:0000269|PubMed:3108233}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P0AEK7};
CC -!- SUBUNIT: Composed of three subunits: PhsA, PhsB and PhsC.
CC {ECO:0000305|PubMed:22081391}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:22081391}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the PhsC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA68434.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L32188; AAC36936.1; -; Genomic_DNA.
DR EMBL; L31538; AAA68433.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L31538; AAA68434.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE006468; AAL20967.1; -; Genomic_DNA.
DR PIR; C57143; C57143.
DR RefSeq; NP_461008.1; NC_003197.2.
DR RefSeq; WP_001092559.1; NC_003197.2.
DR AlphaFoldDB; P37602; -.
DR SMR; P37602; -.
DR STRING; 99287.STM2063; -.
DR TCDB; 5.A.3.5.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PaxDb; P37602; -.
DR EnsemblBacteria; AAL20967; AAL20967; STM2063.
DR GeneID; 1253584; -.
DR KEGG; stm:STM2063; -.
DR PATRIC; fig|99287.12.peg.2185; -.
DR HOGENOM; CLU_097472_0_0_6; -.
DR PhylomeDB; P37602; -.
DR BioCyc; MetaCyc:MON-12543; -.
DR BioCyc; SENT99287:STM2063-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR InterPro; IPR011577; Cyt_b561_bac/Ni-Hgenase.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF01292; Ni_hydr_CYTB; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Iron; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="Thiosulfate reductase cytochrome B subunit PhsC"
FT /id="PRO_0000058408"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 67
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 /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P0AEK7"
FT BINDING 98
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 /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P0AEK7"
FT BINDING 205
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 /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P0AEK7"
FT BINDING 219
FT /ligand="a menaquinone"
FT /ligand_id="ChEBI:CHEBI:16374"
FT /evidence="ECO:0000250|UniProtKB:P0AEK7"
FT BINDING 219
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 /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P0AEK7"
FT CONFLICT 43..44
FT /note="ML -> IV (in Ref. 2; AAA68433)"
FT /evidence="ECO:0000305"
FT CONFLICT 250..254
FT /note="DKSAV -> ISPPSERIHKIMSARKCALCHIFLQFIHVCLTELP (in
FT Ref. 2; AAA68434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 28547 MW; 46A2DA442EBD5AFD CRC64;
MNTIWGAELH YAPDYWPLWL IYAGVVVLLM LVGLVIHALL RRMLAPKTAG GEEHRDYLYS
LAIRRWHWGN ALLFVLLLLS GLFGHFSLGP VALMVQVHTW CGFALLAFWV GFVLINLTTG
NGRHYRVNFS GLVTRCIRQT RFYLFGIMKG EAHPFVATEQ NKFNPLQQLA YLAIMYALVP
LLIITGLLCL YPQVAGLGPV MLVLHMALAI IGLLFICAHL YLCTLGDTPG QIFRSMVDGY
HRHRTAPRGD KSAV
