ID A0A1Q5NDE6_9ACTN Unreviewed; 862 AA.
AC A0A1Q5NDE6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Transporter {ECO:0000313|EMBL:OKK24446.1};
GN ORFNames=AMK09_06475 {ECO:0000313|EMBL:OKK24446.1};
OS Streptomyces sp. CB02488.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703920 {ECO:0000313|EMBL:OKK24446.1, ECO:0000313|Proteomes:UP000186200};
RN [1] {ECO:0000313|EMBL:OKK24446.1, ECO:0000313|Proteomes:UP000186200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02488 {ECO:0000313|EMBL:OKK24446.1,
RC ECO:0000313|Proteomes:UP000186200};
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:OKK24446.1}.
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DR EMBL; LIVO01000002; OKK24446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5NDE6; -.
DR STRING; 1703920.AMK09_06475; -.
DR Proteomes; UP000186200; 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; 2.
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:UP000186200};
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..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..251
FT /note="SLC26A/SulP transporter"
FT /evidence="ECO:0000259|Pfam:PF00916"
FT DOMAIN 276..375
FT /note="SLC26A/SulP transporter"
FT /evidence="ECO:0000259|Pfam:PF00916"
FT REGION 254..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 88842 MW; BBFBDADF337BAF9A CRC64;
MSASITVFLL AIPMSLGLAV AMDAPLEAGL ISAAVGGIVA GLLGGTPLQV SGPSAGLTVV
TAELIQVYGW RTTCAITIGA GLLQILLGSL RAARSALAVS PAIVHGTLAG IGVAIALAQL
HIVLGGSPES SAVSNALTLP ARLEQVVPAA PLIGGLTVVI LVLWPRIPGR PGRIMRRVPA
ALVSVAAATA VAAFAAPSIA RVDLPSWRSH ALPEMPQGPV LGLATAVFTM MLVASLESLL
AAVAVDKLAA DRNSERTADL PEPGSGPTAS PPLKRSDLDR ELRAQGIANA VSGLLGGLAV
SGGAVRSSAN VRAGATSRAS TVLHGVWVLL ATGLLVTALE WIPLAALGAL VMVVGIQMVN
FAHIRNVHRH REFLVYGATI SGVLLFGVLK GVAIGIAVAV AVALHRLART RITVTEQDGR
HLVVVRGQLT FLAVPRLNRT LGQLPQDADV LVELDGFFID HAAYEMIQDW GNAHAAHGGR
VVFAGRSGGR IAEPSSAAHS CCRPWTPWRN HHCHDGPDPA GLATYAGSTE PAGTITDPGP
APATGATDNP APLHPGPIPT PPPSDGTDST GGTDSTNITG AAPDGLSHSG TQHSGTQGPG
TQPPPAPPAD YTPDHDAAPA RRTGGQRLVS GLSSFQRNTA PLVREELARL AREGQRPSQL
FITCADSRLV TSMITASGPG DLFTVRNIGN LVPPPHSESG DDSVGAAIEY AVDVLGVESI
TICGHSGCGA MNALLGAGPG TPDTPLWRWL RHGVPSLKRM ASKRHAWARI SGRLPADEVE
QLCLTNVVQQ LDHLRAHGSV ARRLAEGTLQ LHGMYFHVAE AQSYLLTEGI GAGHGLDEVF
DRVGPSAPYD PYEPAELART GA
//
