ID W0BDQ0_9GAMM Unreviewed; 769 AA.
AC W0BDQ0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Sulfate permease-related transporters MFS superfamily {ECO:0000313|EMBL:AHE66544.1};
DE EC=4.2.1.1 {ECO:0000313|EMBL:AHE66544.1};
GN ORFNames=Loa_00988 {ECO:0000313|EMBL:AHE66544.1};
OS Legionella oakridgensis ATCC 33761 = DSM 21215.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE66544.1, ECO:0000313|Proteomes:UP000018838};
RN [1] {ECO:0000313|EMBL:AHE66544.1, ECO:0000313|Proteomes:UP000018838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA Heuner K.;
RT "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT characterization reveals its replication capacity in amoebae.";
RL Int. J. Med. Microbiol. 303:514-528(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000256|ARBA:ARBA00008692}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217}.
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DR EMBL; CP004006; AHE66544.1; -; Genomic_DNA.
DR RefSeq; WP_025385307.1; NZ_CP004006.1.
DR AlphaFoldDB; W0BDQ0; -.
DR STRING; 1268635.Loa_00988; -.
DR KEGG; lok:Loa_00988; -.
DR PATRIC; fig|1268635.3.peg.984; -.
DR eggNOG; COG0288; Bacteria.
DR eggNOG; COG0659; Bacteria.
DR HOGENOM; CLU_003182_11_1_6; -.
DR Proteomes; UP000018838; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR PANTHER; PTHR11814:SF215; C4-DICARBOXYLIC ACID TRANSPORTER DAUA; 1.
DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AHE66544.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018838};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..388
FT /note="SLC26A/SulP transporter"
FT /evidence="ECO:0000259|Pfam:PF00916"
SQ SEQUENCE 769 AA; 84535 MW; 20DF6BB5DAF65618 CRC64;
MTEALSTNFR KLRVYKRRAL KFDFIAAIVV FLVAIPLCLG IALASGAPLF SGILSGIIGG
IVVGSLSGSQ VSVSGPAAGM AAVVLAAIAQ LGDFNTFLLA LTLAGLLQIM VGSLRAGFIA
DYVPSNVIQG LLCAIGLLLI IKQLPLAFTL SSDLAELKMH LLETTEGLTL KPLYELSFHI
NSGAMLLSLI SFAILIFFSK TNIAWLKVIP GPIVVVIAGI ILNELFVLSD SYLAQNSPQL
VNIPEHDGFS DFLSQLQSPT WSAWNNPKVY LYAFILATVA SLESLLNVKA GEKLDRKRRY
CSKDQELFAQ GFGNLISGLI GGIPITSVIV RTSVNIQAGS KTKVSTILHG LFILFAVMLI
PQALNKIPLS SLAAILIYTG YKLTSPSIYL NIFRQGLDRF IPFIATVISI VVFNLLAGIL
LGLLVSLFYI LKSNSQVRLD IIKEFYPNGV TNRLILPQQT TFLNKASLVA ELDSIPRNSQ
LIIDARYSDY IDKEIVEFLK EFKNEQAPHK QLSLNLIGFK DHYAIHNYID FINVTTYDVQ
SMLKPSQVLN ILKEGNQRFL HDNRIHRSIK TDIKYTATTQ HPIAVVLGCI DSRVPVETIF
DMSFGDLFCV RVAGNVVNDD VLASIEYACH VVGAKLIVVL GHTRCGAIQA ACDNVEQGHI
TQLLAKIKPA ITAETQTAQN RTSKNSDFVY HVTELNIANT LQHIYQESKI LSTMMNHEDI
SMVGAVYDVH TGEVKFKDFS AEVTYFDKKH SNQLAEKLHK LIHEANSEH
//
