ID   A0A164P253_9NOCA        Unreviewed;       749 AA.
AC   A0A164P253;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Carbonic anhydrase {ECO:0000313|EMBL:KZF08781.1};
GN   ORFNames=A2J03_00505 {ECO:0000313|EMBL:KZF08781.1};
OS   Rhodococcus sp. EPR-157.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF08781.1, ECO:0000313|Proteomes:UP000077673};
RN   [1] {ECO:0000313|EMBL:KZF08781.1, ECO:0000313|Proteomes:UP000077673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPR-157 {ECO:0000313|EMBL:KZF08781.1,
RC   ECO:0000313|Proteomes:UP000077673};
RA   Ploux O.;
RL   Submitted (MAR-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:KZF08781.1}.
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DR   EMBL; LVCV01000220; KZF08781.1; -; Genomic_DNA.
DR   RefSeq; WP_068372903.1; NZ_LVCV01000220.1.
DR   AlphaFoldDB; A0A164P253; -.
DR   OrthoDB; 9771198at2; -.
DR   Proteomes; UP000077673; 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:UP000077673};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        247..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        379..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..374
FT                   /note="SLC26A/SulP transporter"
FT                   /evidence="ECO:0000259|Pfam:PF00916"
SQ   SEQUENCE   749 AA;  77588 MW;  15145BDB9ECF1B32 CRC64;
     MTTTVDNESP ESSTDSERTS RIGGILKYDV PASLVVFLVA VPLSIGIAVA SGAPVMAGLI
     AAVVGGILAG ALGGSPLQVS GPAAGLTVVV AELVNQFGWA LTCLITVGAG AVQILLGLSR
     IARHALAISP VVVHAMLAGI GVTIALQQIH VLLGGESESS AVENLLAIPT SVAAGQWPSI
     LVGGVVIALM LLWPRLPGMA SKIPAALVAV VTATAISVVL NLDVERIDLP GNLIEALSLP
     ALPDGQWVGI ATGVLTIALI ASVESLLSAV AVDKMHTGPR TNFDRELLGQ GAANMVSGAA
     GGLPVTGVIV RSSSNVKAGA KSRASAILHG VWILVFSVLF ISIVELVPFA ALAGLLVMIG
     VQLIKLADIR IASKTGDIAV YSVTVIGVVV LNLLEGVLIG LALAVFLVLR RVVWAHVRAS
     ETVDGTWRVH MEGSLSFLSL PRLTHVLSSV PSGAKVNMEL AVDFLDHAVH EHLHEWVRQH
     ELGGGDVSIE ENGSASLAAA AEGPPKRGMA GVRGSLAPWS AWQLKSDSEV NENPPALRPV
     LSGVAEYHRT HADAIKPHLQ GMKEFQDPDT FFLCCVDSRV MPNTITSSGP GDLFTVRNMG
     NMIPAQGQDT SVEASLAYGV DILGTSSVVV CGHSGCGAMR AILAGPDTVG DERVVEWLEH
     GLASLEALRS GHPVGRAAAE LGFAEGDQLA MVNVAVQLQT LTRHRVVGRA AAEGKLRVTG
     LFFDIPSARV LQISTKEITV LDTAEVEPV
//