ID A0A0F7N753_9ACTN Unreviewed; 844 AA.
AC A0A0F7N753;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Transporter {ECO:0000313|EMBL:AKH83224.1};
GN ORFNames=AA958_14390 {ECO:0000313|EMBL:AKH83224.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH83224.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH83224.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH83224.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide to form
CC bicarbonate. {ECO:0000256|ARBA:ARBA00024993}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217}.
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DR EMBL; CP011492; AKH83224.1; -; Genomic_DNA.
DR RefSeq; WP_047016540.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7N753; -.
DR STRING; 444103.AA958_14390; -.
DR KEGG; strc:AA958_14390; -.
DR PATRIC; fig|444103.5.peg.3028; -.
DR OrthoDB; 9771198at2; -.
DR Proteomes; UP000034283; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
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:SF227; CARBONIC ANHYDRASE; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..430
FT /note="SLC26A/SulP transporter"
FT /evidence="ECO:0000259|Pfam:PF00916"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 87014 MW; 8B69B7EA53567986 CRC64;
MPAGRPTPLG SPSAERAKDP EHEPEHEPEH TADPAPPKTA GHAGHAAVPG PAGPSEHTAP
RRPFVADLSA SVTVFLIALP LSLGIALATG APLQAGLLSA AVGGIVVGLI GGAPLQVSGP
AAGLTVVTAD LIQQYGWRTT CAITAFAGLA QLALGSLRVA RAALAVSPAI VHGMLAGIGA
TIALAQLHIV LGGSPQSSPV DNTLALPGQF ADLDPAAVSV SAVVIVVLLG WPWLRGRGTG
PLRYVPGALA AIVLATGFAS LTGLRLPRVD LPSWSSHALA GVPDGPVLGL VAAVLTITVV
ASVESLLSAV AVDKLAVARG DRHPVPRTDL DRELRAQGAG NFFAGLLGGL PITGVAVRSS
ANVAAGAVGR RSAVLHGVWV VLASLLLVGM LELIPLAALG ALVMVVGIQM VKISHVRSVR
RHREVLVYAA TVAGVVMLGV LEGVAVGIAV AVAMSLHRLS RTRVTLERRG GDAAPGAAGE
GGPEDTYLVR VRGQLTFLAV PRLSRGLAQV PPGATVEVEL TGSFMDHAAY ETLQEWRQAH
IAHGGAAELV SATGRRIAEP ATAHHCHPWT PWRNHCCVTS PEQPAPAHRL LSGISNFQRN
TAPRVREELA RLAREGQRPT QLFLTCADSR VVTSMITSSG PGDLFTVRNV GNLVPLPDEP
GDRAGSASDA DGGTATPGTR RDATLQDDSV AAAIEFAVEV LRVESITVCG HSGCGAVQAL
LDEEAAHGGA ADPAAGVPPT PLRRWLRHGL PSLARARADG PRIVSRPFAD DTERVSVANV
AQQLDHLRRH PCVRRRLADG SLSLHGMYFH VGEAQAYVLG EQGDFTAVRP GPAGLAERAA
ADVR
//
