ID CYSZ_SHIFL Reviewed; 253 AA.
AC Q83QN8;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE RecName: Full=Sulfate transporter CysZ {ECO:0000255|HAMAP-Rule:MF_00468};
GN Name=cysZ {ECO:0000255|HAMAP-Rule:MF_00468};
GN OrderedLocusNames=SF2468, S2614;
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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. {ECO:0000255|HAMAP-Rule:MF_00468}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00468}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00468}.
CC -!- SIMILARITY: Belongs to the CysZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00468}.
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DR EMBL; AE005674; AAN43975.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17788.1; -; Genomic_DNA.
DR RefSeq; NP_708268.1; NC_004337.2.
DR RefSeq; WP_000254831.1; NZ_CP123365.1.
DR AlphaFoldDB; Q83QN8; -.
DR SMR; Q83QN8; -.
DR STRING; 198214.SF2468; -.
DR PaxDb; 198214-SF2468; -.
DR GeneID; 1027218; -.
DR KEGG; sfl:SF2468; -.
DR KEGG; sfx:S2614; -.
DR PATRIC; fig|198214.7.peg.2949; -.
DR HOGENOM; CLU_070331_1_0_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR HAMAP; MF_00468; CysZ; 1.
DR InterPro; IPR022985; Sulfate_CysZ.
DR PANTHER; PTHR37468; SULFATE TRANSPORTER CYSZ; 1.
DR PANTHER; PTHR37468:SF1; SULFATE TRANSPORTER CYSZ; 1.
DR Pfam; PF07264; EI24; 1.
PE 3: Inferred from homology;
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_0000204350"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00468"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00468"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00468"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00468"
FT CONFLICT 190
FT /note="T -> N (in Ref. 2; AAP17788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 29354 MW; 796661C30FF4E56F CRC64;
MVSSFTSAPR SGFYYFAQGW KLVSQPGIRR FVILPLLVNI LLMGGAFWWL FTQLDVWIPT
FMSYVPDWLQ WLSYLLWPLA VISVLLVFGY FFSTIANWIA APFNGLLAEQ LEARLTGATP
PDTGIFGIMK DVPRIMKREW QKFVWYLPRA IVLLILYFIP GIGQTVAPVL WFLFSAWMLA
IQYCDYPFDT HKVPFKEMRT ALRTRKITNM QFGALTSLFT MIPLLNLFIM PVAVCGATAM
WVDCYRDKHA MWR
//
