ID A0A1V9KD10_9ACTN Unreviewed; 788 AA.
AC A0A1V9KD10;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE SubName: Full=Transporter {ECO:0000313|EMBL:OQQ17468.1};
GN ORFNames=B0675_10385 {ECO:0000313|EMBL:OQQ17468.1};
OS Streptomyces sp. M41(2017).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1955065 {ECO:0000313|EMBL:OQQ17468.1, ECO:0000313|Proteomes:UP000192467};
RN [1] {ECO:0000313|EMBL:OQQ17468.1, ECO:0000313|Proteomes:UP000192467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:OQQ17468.1,
RC ECO:0000313|Proteomes:UP000192467};
RX PubMed=28326787; DOI=10.1021/acs.orglett.7b00545;
RA Wyche T.P., Ruzzini A.C., Beemelmanns C., Kim K.H., Klassen J.L., Cao S.,
RA Poulsen M., Bugni T.S., Currie C.R., Clardy J.;
RT "Linear Peptides Are the Major Products of a Biosynthetic Pathway That
RT Encodes for Cyclic Depsipeptides.";
RL Org. Lett. 19:1772-1775(2017).
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:OQQ17468.1}.
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DR EMBL; MWFK01000001; OQQ17468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9KD10; -.
DR STRING; 1955065.B0675_10385; -.
DR OrthoDB; 9771198at2; -.
DR Proteomes; UP000192467; 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:UP000192467};
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..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..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..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 82052 MW; 14F879896BD3612C CRC64;
MSACVPTRAA DPTRPARTHE PHSPPPPPPR RFRIESADLS ASIAVFLIAL PLSLGIALAT
GAPLQAGLVA AAVGGLVAGR IGGSALQVSG PAAGLTVVTA ELIHHYGWRA TCGITVLAGI
TQLGLGCLRV ARTALAVSPA IVHGMLAGIG VTIAVAQLHI VLGGVPQSSV LANLVGLPDQ
VARMQPAAVS MSVLTLVLLF AWPRLPGRTG RLLRKVPAAL VAVAGATATA SLAGLTLPRV
DLPSWSSHAL AGLPEGPVLG VAAAVLTVTL VCSVQSLLGA VAVDKLVSAR PELQARVGRS
ALDRELLGQG AANVVSGALG GLPVAGVAVR SSANVQAGAV SRNSTMLHGV FVVVAALLMV
PILELIPLAS LAALVMAVGI QMVSLHHIRT VTRHREVLVY AVTTLGVVFL GVLEGVALGV
AVAVGVALHR LTRTRITHEE REGVHHVRVR GQLTFLAVPR LSRALHLIPR GADTVVELDG
SFMDHAAFES LQDWQSAHSA QGGSVEITGR AGTRIAEPAD STHCRCRPWT PWRNHHCEDP
SAMESASSGA PSDGRDEESP EPRPSGHQLA RGISAFQRNT APLVREELAR LAREGQRPSQ
LFLTCADSRL VTSMITSSGP GDLFVVRNVG NLVPLPGEES GDDSVAAAIE YAVDVLKVRS
ITVCGHSGCG AMQALLASEP GGALTPLKRW LRHGRPSVER MADEGRTKPR LTGRAPADTV
EQLCLTNVVQ QLEHLRAHDS VARALNEGAL ELHGMYFHVG EAQAYLLADD EAELFGHVGA
ADDLRHPA
//
