ID A0A022MCL9_9ACTN Unreviewed; 849 AA.
AC A0A022MCL9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Transporter {ECO:0000313|EMBL:EYT80271.1};
GN ORFNames=CF54_26495 {ECO:0000313|EMBL:EYT80271.1};
OS Streptomyces sp. Tu 6176.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT80271.1, ECO:0000313|Proteomes:UP000020060};
RN [1] {ECO:0000313|EMBL:EYT80271.1, ECO:0000313|Proteomes:UP000020060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT80271.1,
RC ECO:0000313|Proteomes:UP000020060};
RA Olano C., Cano-Prieto C., Mendez C., Salas J.A.;
RT "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the
RT cytotoxic benzoxazol nataxazol.";
RL Submitted (MAR-2014) 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:EYT80271.1}.
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DR EMBL; JFJQ01000852; EYT80271.1; -; Genomic_DNA.
DR RefSeq; WP_037894244.1; NZ_KK106991.1.
DR AlphaFoldDB; A0A022MCL9; -.
DR HOGENOM; CLU_003182_11_0_11; -.
DR OrthoDB; 9771198at2; -.
DR Proteomes; UP000020060; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..391
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 539..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 86435 MW; CFC5C7CA09253505 CRC64;
MPARTPSPTG TARTRRAHPP HSPPPRRRLP RVAGADLSAA VAVFLIALPL SLGIALATGA
PLQAGLVAAA VGGLVAGRLG GSPLQVSGPA AGLTVVTADL IHRYGWRTTC AITVLAGLLQ
LALGCLRVAR AALAVSPAVV HGMLAGIGLT IAVAQLHIVL GGSPQSSVPD NLRALPSQLA
GADPAALAVG ALTLALLLSW PRLPGRAGRL LRPVPAALVA VTGATAVASL CGLILPRVDL
PSWRSHALAG LSDGPVLGLV AAVLSTTLVC SVQSLLGAVA VDRLAAGRPG PPVPAARSDL
DRELLGQGAA NVVSGALGGL PVAGVAVRSS ANVRAGAVSR DATMLHGALV VAAALLLVPV
LEFIPLAALA ALVMAVGVQM VSLHHIRTVA RHREVPVYAV TALGVVALGV LQGVALGVAT
AVAVALHRLA RTRITHDERK GVHHVRVRGQ LTFLAVPRLS RVLHRVPRGA VSVVELDGSF
MDHAAYESLQ DWQRAHTAQG GSVRLTGRRR AVRVGEPTGP DGAACRCRPW TPWRNHQCPA
PGIRSEVRPT PGAPSRAAGS PGPSGEQLAR GIGVFQRTTA PHVRDELARL AREGQQPSHL
FLTCADSRLV TSMITASGPG DLFVVRNVGN LVPLPGQERG DDSVAAGIEY AVDVLGVRSL
TVCGHSGCGA MQALLGSRPG TGDDGTSLGR WLRHGAPSLE RLRATDGTVP LLAGRMPADE
TERLSLANVV QQLEHLRAHD PVARALRAGT LELHGMYFQV AEAQAYLLTD PAGDRDGGAV
FVPVAAEEAE EAAEAAGPAE APQTAEVAGA AGAAAQEAPA AGTAGPPGAP AGPDAPRPTE
SAKDLPSAV
//
