ID A0A1S2P7S4_9ACTN Unreviewed; 793 AA.
AC A0A1S2P7S4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Transporter {ECO:0000313|EMBL:OIJ89741.1};
GN ORFNames=BIV24_19155 {ECO:0000313|EMBL:OIJ89741.1};
OS Streptomyces colonosanans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428652 {ECO:0000313|EMBL:OIJ89741.1, ECO:0000313|Proteomes:UP000179935};
RN [1] {ECO:0000313|EMBL:OIJ89741.1, ECO:0000313|Proteomes:UP000179935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 93 {ECO:0000313|EMBL:OIJ89741.1,
RC ECO:0000313|Proteomes:UP000179935};
RA Lee L.-H., Ser H.-L., Law J.W.-F.;
RT "Genome sequence of Streptomyces sp. MUSC 93.";
RL Submitted (OCT-2016) 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}.
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:OIJ89741.1}.
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DR EMBL; MLYP01000049; OIJ89741.1; -; Genomic_DNA.
DR RefSeq; WP_071367573.1; NZ_MLYP01000049.1.
DR AlphaFoldDB; A0A1S2P7S4; -.
DR STRING; 1428652.BIV24_19155; -.
DR OrthoDB; 9771198at2; -.
DR Proteomes; UP000179935; 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 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:UP000179935};
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..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..86
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..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..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 303..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..399
FT /note="SLC26A/SulP transporter"
FT /evidence="ECO:0000259|Pfam:PF00916"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 82452 MW; F462D74F482466FF CRC64;
MPACVPAHAT DSTQTKRLHQ PHSPPPTPPH RFRVAGADLS ASIAVFLIAL PLSLGIALAT
GAPLQSGLVA AAIGGLVAGL LGGSPLQVSG PAAGLTVVTA DLIHHYGWRT TCAITVLAGF
AQLGLGCLRV ARTALAVSPA IVHGMLAGIG VTIAMAQLHI VLGGTPQSAV LDNLQALPAQ
LARLHPAAVS VSALTLAVLL LWPRLPGRTG RILRKIPAAL VAVTAATTTA SLAGFTLPKV
DLPSWNSHAL AGLPEGPALG IAAAVLTITL VCSVQSLLGA VAVDKLAAGR HPHLGRSDLN
RELLGQGAAN IVSGALGGLP LAGVAVRSSA NVQSGATSRN STMLHGVWVV VAALLMVPVL
ELVPLASLAA LVMAVGIQMV SLHHIRTVTR HREVLVYAVT TLGVVFLGVL QGVTLGVAVA
VAVALHRLAR TRITHEETEG VHYVRVRGQL TFLAVPRLSR TLHLLPVGAD AVVELDGSFM
DHAAYESLQD WQKTHRARGG TVDLTGRAGT RIAKPAPNAP SLTGDQETAE APACRCRPWT
PWRNHQCERS PSTPADGHPG GPSDGARASE QQLARGISAF QRNTAPQVRH ELARLAREGQ
RPSQLFLTCA DSRLVTSMIT SSGPGDLFVV RNVGNLVPLP GVESGDDSVA AAIEYAVDVL
RVRSITVCGH SGCGAMQALL SSEPGGAQTP LRRWLRHGMP SLEPTADGER PRARISARAP
ADAVEQLCLA NVVQQLEHLR AHGSVARALS EDRLELHGMY FHVGEAQAYL LTPSEDGAVF
ERVGAVGELR SPA
//