ID A0A0F7GC68_9CHLR Unreviewed; 565 AA.
AC A0A0F7GC68;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=RCK N-terminal domain-containing protein {ECO:0000259|PROSITE:PS51201};
GN ORFNames=DGWBC_0362 {ECO:0000313|EMBL:AKG53049.1};
OS Dehalogenimonas sp. WBC-2.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=943347 {ECO:0000313|EMBL:AKG53049.1, ECO:0000313|Proteomes:UP000034106};
RN [1] {ECO:0000313|EMBL:AKG53049.1, ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|EMBL:AKG53049.1,
RC ECO:0000313|Proteomes:UP000034106};
RX PubMed=26452554; DOI=10.1128/AEM.02017-15;
RA Molenda O., Quaile A.T., Edwards E.A.;
RT "Dehalogenimonas sp. Strain WBC-2 Genome and Identification of Its trans-
RT Dichloroethene Reductive Dehalogenase, TdrA.";
RL Appl. Environ. Microbiol. 82:40-50(2015).
RN [2] {ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|Proteomes:UP000034106};
RA Molenda O., Edwards E.A.;
RT "Identification of trans-1,2-dichloroethene reductive dehalogenase (TdrA)
RT in Dehalogenimonas sp. WBC-2.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC transporter (TC 2.A.37) family. {ECO:0000256|ARBA:ARBA00005551}.
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DR EMBL; CP011392; AKG53049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7GC68; -.
DR STRING; 943347.DGWBC_0362; -.
DR KEGG; dew:DGWBC_0362; -.
DR PATRIC; fig|943347.4.peg.373; -.
DR Proteomes; UP000034106; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003148; RCK_N.
DR PANTHER; PTHR42751:SF3; NA(+)_H(+) ANTIPORTER; 1.
DR PANTHER; PTHR42751; SODIUM/HYDROGEN EXCHANGER FAMILY/TRKA DOMAIN PROTEIN; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51201; RCK_N; 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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 413..534
FT /note="RCK N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51201"
SQ SEQUENCE 565 AA; 60677 MW; 0A56DEB3CB2B4C04 CRC64;
MEDLGVGFDL VVVLIAALLG GFLARRLKLP IFLGYLVGGI LIGPSGFRLV EETGIINAVA
QVGLILMLFT IGLEFSLPEL KRTGKVAVWG GIAQVLLTAA AGFGLGKLLG WENAEAIFFG
FIIAQTSTAV TFKALSERGE LDSAHGRIVL GVSLVQDMST VPLLVILPVL AGFEVNLAES
LGLAVGKALL FIIIIIAVGV WVLPRVLKRA AEARSRELFL LFIVVMALLT AVAALVFGLS
VAIGAFVAGV LIGQSIFARQ ALANIIPLRD IFGALFFVSL GMLANLADAF VNPGMLIAII
LFVLLVKFVI CAIIPWVFGY GSRTSILAGM GLIPMGEFSF ILASTGLALA VVSDSLFSIT
LTLVAVTMVL SPFLMNLGAR LHRWLSHNKL TQQITASRAE VEWLSGKTTM SGHAVICGHG
RTAAPLTKVL KRRNLSYLVI ELDPQKITQL RREGVPCIYG DASNPEILAV AHLEKARLLV
CTFPSFFDVE ATVRNALLIN PKLDIVAKVD RDQDADELKV AGVNELVKPQ FETSMEMTRH
TLQRYGVPNT EIQLILSSLR QGTMS
//
