ID A0A1Q5KDD7_9ACTN Unreviewed; 898 AA.
AC A0A1Q5KDD7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Transporter {ECO:0000313|EMBL:OKJ79594.1};
GN ORFNames=AMK31_26475 {ECO:0000313|EMBL:OKJ79594.1};
OS Streptomyces sp. TSRI0107.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ79594.1, ECO:0000313|Proteomes:UP000185813};
RN [1] {ECO:0000313|EMBL:OKJ79594.1, ECO:0000313|Proteomes:UP000185813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ79594.1,
RC ECO:0000313|Proteomes:UP000185813};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKJ79594.1}.
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DR EMBL; LIVZ01000010; OKJ79594.1; -; Genomic_DNA.
DR RefSeq; WP_073943231.1; NZ_LIVZ01000010.1.
DR AlphaFoldDB; A0A1Q5KDD7; -.
DR STRING; 1703942.AMK31_26475; -.
DR OrthoDB; 9771198at2; -.
DR Proteomes; UP000185813; Unassembled WGS sequence.
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 Gene3D; 3.30.750.24; STAS domain; 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 InterPro; IPR036513; STAS_dom_sf.
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.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000185813};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..402
FT /note="SLC26A/SulP transporter"
FT /evidence="ECO:0000259|Pfam:PF00916"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 92496 MW; 9D9F1D83E55B740F CRC64;
MSACVPTRPT DPHQSNRSHQ PHSPPSRGPL RSRIAGADVS ASIAVFLIAL PLSLGIALAT
GAPLQAGLVA AAVGGIVVGR LGGSPLQVSG PAAGLTVVTA DLIHLYGWRT TCAITVLAGL
SQLGLGCLRV ARTALAVSPA IVHGMLAGIG VTIAVAQLHI VLGGTPQSAV LDNLRALPAQ
LAQLHPAALS MSALTLTLLF VWPRLPGRAG RLLRKAPAPL IAVAGATSTA SLAGLTLPKV
DLPSWSNHAL AGRPEGPVLG LIAAVLTITL VCSVQSLLGA VAVDKLAAAR PGLTGRVPRS
DLDRELLGQG AANMVSGALG GLPVAGVAVR STANVNSGAV SRNSTMLHGV LVVVAALLMV
PLLELIPLAS LAALVMAVGI QMVSLHHIRT VTRHREVLVY AVTTLGVVLF GVLEGVALGI
AVAVAVALHR LTRTRITHTE EKGVHHVHVR GQLTFLAVPR LSRMLHHVPQ GTDVVVELDG
SFMDHAAYET LQDWQNTHTA QGGTVELTGR RAGIRIAEPG APSEPHTGTD ADDPEGAGDC
RCRPWTAWRN HQCEWERPVP EPAADAGTGR VRGDGPDGSE DADITGGTED SGGTGDPRGP
GSSGQSAAGV TGPADPEDPG SPDGSGRPGG TGRPGSSGRA EDSDSPRARQ NPTGSAPSAP
SAPSTGSASA DSPGGHHLAR GISAFQRKTA PLVRGELARL AREGQRPVQL FLTCADSRLV
TSMITSSGPG DLFVVRNVGN LVPLPGEESG DDSVAAAIEY AVDVLEVRSI TVCGHSGCGA
MQALINSEPG GAQTPLKRWL RHGMPSLERM ADTERPWARL AGRRPADAVE QLCLTNVVQQ
LEHLRAHESV ARALREGALE LHGMYFHVGE AQAYLLTEAA GAEVFDHVPD AEDLRSPA
//
