ID B4ETM5_PROMH Unreviewed; 566 AA.
AC B4ETM5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Sulfate transporter {ECO:0000313|EMBL:CAR42361.1};
GN OrderedLocusNames=PMI1093 {ECO:0000313|EMBL:CAR42361.1};
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR42361.1, ECO:0000313|Proteomes:UP000008319};
RN [1] {ECO:0000313|EMBL:CAR42361.1, ECO:0000313|Proteomes:UP000008319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR42361.1,
RC ECO:0000313|Proteomes:UP000008319};
RX PubMed=18375554; DOI=10.1128/JB.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362052}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362052}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000256|ARBA:ARBA00008692, ECO:0000256|RuleBase:RU362052}.
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DR EMBL; AM942759; CAR42361.1; -; Genomic_DNA.
DR RefSeq; WP_004247967.1; NC_010554.1.
DR AlphaFoldDB; B4ETM5; -.
DR EnsemblBacteria; CAR42361; CAR42361; PMI1093.
DR GeneID; 6800826; -.
DR KEGG; pmr:PMI1093; -.
DR PATRIC; fig|529507.6.peg.1057; -.
DR eggNOG; COG0659; Bacteria.
DR HOGENOM; CLU_003182_13_1_6; -.
DR Proteomes; UP000008319; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR InterPro; IPR018045; S04_transporter_CS.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR NCBIfam; TIGR00815; sulP; 1.
DR PANTHER; PTHR11814:SF215; C4-DICARBOXYLIC ACID TRANSPORTER DAUA; 1.
DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362052};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362052};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362052}; Transport {ECO:0000256|RuleBase:RU362052}.
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 100..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 172..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 210..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 279..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 360..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 410..440
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 452..562
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 566 AA; 60391 MW; 133C2E7B505ACD57 CRC64;
MKTHKVNRVR PFSAFIDACV KEPYSFARLL KDIIAGITVG IIAIPLAMAL AIGSGVPPQY
GLYTAAIAGI IIAVTGGSRY SVSGPTAAFV VILYPVSQQF GLSGLLIATL MSGIILVVMG
LARFGKLIEY IPVSVTLGFT SGIAITIATM QIKDFFGLEM SHVPETYIDK VIALGAALPT
IHLGDTLIGV TTLLVLIYWP KLNLRLPGHL PALIAGTAVM GIVNLFGHDV ATIGSQFSYL
LPDGSTGQGI PPILPQFVLP WNLPSSGESI ALNWSTVSAL LPAAFSMAML GAIESLLCAV
VLDGMTGKKH HSNGELVGQG IGNIVAPFFG GITATAAIAR SAANVRAGAT SPVSAIVHSL
LVLVTLLVLA PFLSYLPLAA MSALLLIVAW NMSEARKVID LIRHAPKDDI IVLVLCLSLT
VLFDMVIAIT IGIVLASLLF MRRIANMTKI TESTYTDDDK QLLVVRVNGP LFFAAAERIF
NELRERSKGY KTLIMQWDAV PVLDAGGLHA FQHFVADVQH DTHIIVCDIP FQPLKTLARA
RVTPIDGTLN FYPSLQKALD DMELIQ
//
