CYSZ_ECOLI
ID CYSZ_ECOLI Reviewed; 253 AA.
AC P0A6J3; P12610; P76533; P76961; P76962;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Sulfate transporter CysZ {ECO:0000255|HAMAP-Rule:MF_00468, ECO:0000303|PubMed:24657232};
GN Name=cysZ {ECO:0000255|HAMAP-Rule:MF_00468, ECO:0000303|PubMed:3290198};
GN OrderedLocusNames=b2413, JW2406;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RC STRAIN=PB103;
RX PubMed=9008158; DOI=10.1016/s0092-8674(00)81838-3;
RA Hale C.A., de Boer P.A.J.;
RT "Direct binding of FtsZ to ZipA, an essential component of the septal ring
RT structure that mediates cell division in E. coli.";
RL Cell 88:175-185(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-253.
RC STRAIN=K12;
RX PubMed=3290198; DOI=10.1128/jb.170.7.3150-3157.1988;
RA Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M.;
RT "DNA sequences of the cysK regions of Salmonella typhimurium and
RT Escherichia coli and linkage of the cysK regions to ptsH.";
RL J. Bacteriol. 170:3150-3157(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-253.
RX PubMed=3062311; DOI=10.1111/j.1365-2958.1988.tb00089.x;
RA Levy S., Danchin A.;
RT "Phylogeny of metabolic pathways: O-acetylserine sulphydrylase A is
RT homologous to the tryptophan synthase beta subunit.";
RL Mol. Microbiol. 2:777-783(1988).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12;
RX PubMed=24657232; DOI=10.1016/j.bbamem.2014.03.003;
RA Zhang L., Jiang W., Nan J., Almqvist J., Huang Y.;
RT "The Escherichia coli CysZ is a pH dependent sulfate transporter that can
RT be inhibited by sulfite.";
RL Biochim. Biophys. Acta 1838:1809-1816(2014).
CC -!- FUNCTION: High affinity, high specificity proton-dependent sulfate
CC transporter, which mediates sulfate uptake. Provides the sulfur source
CC for the cysteine synthesis pathway. Does not transport thiosulfate.
CC {ECO:0000269|PubMed:24657232}.
CC -!- ACTIVITY REGULATION: Inhibited by sulfite.
CC {ECO:0000269|PubMed:24657232}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.72 uM for sulfate {ECO:0000269|PubMed:24657232};
CC KM=1.3 uM for sulfate (in the presence of 5 uM sulfite)
CC {ECO:0000269|PubMed:24657232};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00468, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00468}.
CC -!- SIMILARITY: Belongs to the CysZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00468, ECO:0000305}.
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DR EMBL; U00096; AAC75466.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16287.2; -; Genomic_DNA.
DR EMBL; U74650; AAB42060.1; -; Genomic_DNA.
DR EMBL; M21451; AAA23653.1; -; Genomic_DNA.
DR EMBL; X12615; CAA31136.1; -; Genomic_DNA.
DR PIR; D65015; BVECCZ.
DR RefSeq; NP_416908.1; NC_000913.3.
DR RefSeq; WP_000254839.1; NZ_SSZK01000005.1.
DR AlphaFoldDB; P0A6J3; -.
DR SMR; P0A6J3; -.
DR BioGRID; 4259702; 13.
DR STRING; 511145.b2413; -.
DR TCDB; 2.A.121.1.1; the sulfate transporter (cysz) family.
DR jPOST; P0A6J3; -.
DR PaxDb; P0A6J3; -.
DR PRIDE; P0A6J3; -.
DR DNASU; 946875; -.
DR EnsemblBacteria; AAC75466; AAC75466; b2413.
DR EnsemblBacteria; BAA16287; BAA16287; BAA16287.
DR GeneID; 946875; -.
DR KEGG; ecj:JW2406; -.
DR KEGG; eco:b2413; -.
DR PATRIC; fig|1411691.4.peg.4318; -.
DR EchoBASE; EB0003; -.
DR eggNOG; COG2981; Bacteria.
DR HOGENOM; CLU_070331_1_0_6; -.
DR InParanoid; P0A6J3; -.
DR OMA; PFADDWS; -.
DR PhylomeDB; P0A6J3; -.
DR BioCyc; EcoCyc:EG10003-MON; -.
DR SABIO-RK; P0A6J3; -.
DR PRO; PR:P0A6J3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0009675; F:high-affinity sulfate:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0019344; P:cysteine biosynthetic process; IDA:EcoCyc.
DR GO; GO:0000103; P:sulfate assimilation; IMP:EcoCyc.
DR GO; GO:1902358; P:sulfate transmembrane transport; IDA:EcoCyc.
DR HAMAP; MF_00468; CysZ; 1.
DR InterPro; IPR022985; Sulfate_CysZ.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cell inner membrane; Cell membrane;
KW Cysteine biosynthesis; Membrane; Reference proteome; Sulfate transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..253
FT /note="Sulfate transporter CysZ"
FT /id="PRO_0000204336"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00468"
FT TOPO_DOM 52..74
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00468"
FT TOPO_DOM 96..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00468"
FT TOPO_DOM 172..221
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00468"
FT TOPO_DOM 243..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 253 AA; 29305 MW; 057C4908D9FBB453 CRC64;
MVSSFTSAPR SGFYYFAQGW KLVSQPGIRR FVILPLLVNI LLMGGAFWWL FTQLDVWIPT
LMSYVPDWLQ WLSYLLWPLA VISVLLVFGY FFSTIANWIA APFNGLLAEQ LEARLTGATP
PDTGIFGIMK DVPRIMKREW QKFAWYLPRA IVLLILYFIP GIGQTVAPVL WFLFSAWMLA
IQYCDYPFDN HKVPFKEMRT ALRTRKITNM QFGALTSLFT MIPLLNLFIM PVAVCGATAM
WVDCYRDKHA MWR
