PHSB_SALTY
ID PHSB_SALTY Reviewed; 192 AA.
AC P0A1I1; P37601;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Thiosulfate reductase electron transfer subunit PhsB {ECO:0000305};
DE AltName: Full=Thiosulfate reductase subunit beta {ECO:0000305};
GN Name=phsB {ECO:0000303|PubMed:7751291}; OrderedLocusNames=STM2064;
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 PhsB subunit transfers electrons between PhsC and PhsA.
CC {ECO:0000269|PubMed:22081391, ECO:0000269|PubMed:3108233}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P0AAJ3};
CC Note=Binds 4 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P0AAJ3};
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}; Peripheral membrane protein
CC {ECO:0000305|PubMed:22081391}; Periplasmic side
CC {ECO:0000305|PubMed:22081391}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA68432.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; L32188; AAC36935.1; -; Genomic_DNA.
DR EMBL; L31538; AAA68432.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL20968.1; -; Genomic_DNA.
DR PIR; B57143; B57143.
DR RefSeq; NP_461009.1; NC_003197.2.
DR RefSeq; WP_001016236.1; NC_003197.2.
DR AlphaFoldDB; P0A1I1; -.
DR SMR; P0A1I1; -.
DR STRING; 99287.STM2064; -.
DR TCDB; 5.A.3.5.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PaxDb; P0A1I1; -.
DR EnsemblBacteria; AAL20968; AAL20968; STM2064.
DR GeneID; 1253585; -.
DR KEGG; stm:STM2064; -.
DR PATRIC; fig|99287.12.peg.2186; -.
DR HOGENOM; CLU_043374_1_3_6; -.
DR OMA; PHLHFKY; -.
DR PhylomeDB; P0A1I1; -.
DR BioCyc; MetaCyc:MON-12542; -.
DR BioCyc; SENT99287:STM2064-MON; -.
DR BRENDA; 1.8.5.5; 5542.
DR Proteomes; UP000001014; 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 InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF12800; Fer4_4; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
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..192
FT /note="Thiosulfate reductase electron transfer subunit
FT PhsB"
FT /id="PRO_0000159273"
FT DOMAIN 8..36
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 55..86
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 87..116
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 27
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 96
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 139
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 143
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT CONFLICT 77..89
FT /note="PTGASYRDENGIV -> LPERHIVMKTGSL (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21320 MW; 872266242EEEE20C CRC64;
MNHLTNQYVM LHDEKRCIGC QACTVACKVL NDVPEGFSRV QVQIRAPEQA SNALTHFQFV
RVSCQHCENA PCVSVCPTGA SYRDENGIVQ VDKSRCIGCD YCVAACPFHV RYLNPQTGVA
DKCNFCADTR LAAGQSPACV SVCPTDALKF GRLDESEIQR WVGQKEVYRQ QEARSGAVSL
YRRKEVHQEG KA
