ID   K6I807_9LEPT            Unreviewed;       740 AA.
AC   K6I807;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN   ORFNames=LEP1GSC068_3108 {ECO:0000313|EMBL:EKO79745.1};
OS   Leptospira sp. Fiocruz LV3954.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1193012 {ECO:0000313|EMBL:EKO79745.1, ECO:0000313|Proteomes:UP000002809};
RN   [1] {ECO:0000313|EMBL:EKO79745.1, ECO:0000313|Proteomes:UP000002809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz LV3954 {ECO:0000313|EMBL:EKO79745.1,
RC   ECO:0000313|Proteomes:UP000002809};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Selengut J.D., Sanka R., DePew J.,
RA   Ko A.I., Reis M.G., Ribeiro G.S., Wunder E.Jr., Vinetz J.M., Sutton G.G.,
RA   Nelson W.C., Fouts D.E.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544; EC=4.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000943};
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:EKO79745.1}.
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DR   EMBL; AKWV02000016; EKO79745.1; -; Genomic_DNA.
DR   RefSeq; WP_004474393.1; NZ_AKWV02000016.1.
DR   AlphaFoldDB; K6I807; -.
DR   PATRIC; fig|1193012.3.peg.668; -.
DR   Proteomes; UP000002809; 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   CDD; cd00883; beta_CA_cladeA; 1.
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   PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR11002:SF83; CARBONIC ANHYDRASE; 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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..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          16..388
FT                   /note="SLC26A/SulP transporter"
FT                   /evidence="ECO:0000259|Pfam:PF00916"
SQ   SEQUENCE   740 AA;  82698 MW;  5A77B499DD35CD5E CRC64;
     MNILQFFPNV SWNDVRHDFS SSIVVFLVAL PLCIGVAFAS GAPISSGLIS GIVGGAVISL
     ISKSPLSVSG PAMGLTVIVF DSIRTLGSFN DFLFALCLAG VLQIILGFLK AGILSNFFPS
     SVIKGMLAAI GAVLILKQIP HAIGYDMDYE GDMVFFQLDQ ENTFSEILTA LRRFTPGAVV
     LSSVSLVLIV IWEKLELHKK FIIHGSLVAI LVSVLLNETF KIFELGLSVA SEHMIQPIQL
     NGITDLFQGN HFPSFSQWKN QAVYLAALKI CLVMSLETLL NLDAIEKSDP QRRIVSKNRE
     LVAQGTGNLF SAFLGGLPIT SVIIRSSTNL QAGAKTRFSA FLHGLLIFLS LIFIPTWIAK
     IPLASLAAVL LVVGYKLTDY RILKTQYQKG MDQFIPFVAT LIGIVFSDVL IGIGIGCLFS
     VFFIVRRNVL NPYQFNKKEM TYGVEVRIDL SEDVSFLNKS SMLYKLDKVP DNAHLIIDGS
     KSKYIDPDVL EIIEDFKIVA QSRNIKVEII DVTSAYQKIN NKPPDPIAQQ NYQKLFENNR
     IWVKEKLLKD PNYFKNLALG QTPKYLLISC SDSRISVNEM TGTNAGELFV HRNIANLVID
     TDMNLMSVLQ YSVEVLKVEH IVVCGHYGCG GVKAAIDGKY HGLIDAWLRH IKQVYRMNRK
     ELSGILDEDE KHKKLVELNV REQVYNLCKT TIVQNVWSRG TDLQLHGWVY DLKEGKLSDL
     NIDINKDFRD YDIFRYQFET
//