ID   GERN_BACCE              Reviewed;         387 AA.
AC   Q9KI10;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Na(+)/H(+)-K(+) antiporter GerN;
GN   Name=gerN;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN GERMINATION, DISRUPTION
RP   PHENOTYPE, AND GENE NAME.
RC   STRAIN=ATCC 10876 / DSM 9378 / NRRL B-569;
RX   PubMed=11133940; DOI=10.1128/jb.183.2.476-482.2001;
RA   Thackray P.D., Behravan J., Southworth T.W., Moir A.;
RT   "GerN, an antiporter homologue important in germination of Bacillus cereus
RT   endospores.";
RL   J. Bacteriol. 183:476-482(2001).
RN   [2]
RP   FUNCTION AS AN ANTIPORTER, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=ATCC 10876 / DSM 9378 / NRRL B-569;
RX   PubMed=11566988; DOI=10.1128/jb.183.20.5896-5903.2001;
RA   Southworth T.W., Guffanti A.A., Moir A., Krulwich T.A.;
RT   "GerN, an endospore germination protein of Bacillus cereus, is an
RT   Na(+)/H(+)-K(+) antiporter.";
RL   J. Bacteriol. 183:5896-5903(2001).
RN   [3]
RP   FUNCTION IN GERMINATION.
RC   STRAIN=ATCC 10876 / DSM 9378 / NRRL B-569;
RX   PubMed=18641133; DOI=10.1128/jb.00789-08;
RA   Senior A., Moir A.;
RT   "The Bacillus cereus GerN and GerT protein homologs have distinct roles in
RT   spore germination and outgrowth, respectively.";
RL   J. Bacteriol. 190:6148-6152(2008).
CC   -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for
CC       external protons. Can also use potassium as a coupling ion, without
CC       completely replacing H(+). This Na(+)/H(+)-K(+) antiport is much more
CC       rapid than Na(+)/H(+) antiport. Can also extrude lithium. Important for
CC       the inosine-dependent germination of spores.
CC       {ECO:0000269|PubMed:11133940, ECO:0000269|PubMed:11566988,
CC       ECO:0000269|PubMed:18641133}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.5 mM for sodium (at pH 8.0) {ECO:0000269|PubMed:11566988};
CC         KM=25 mM for sodium (at pH 7.0) {ECO:0000269|PubMed:11566988};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11566988}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:11566988}.
CC   -!- DISRUPTION PHENOTYPE: Disruption causes a major defect in inosine-
CC       dependent germination, but does not significantly affect germination in
CC       response to L-alanine. {ECO:0000269|PubMed:11133940}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC       transporter (TC 2.A.37) family. {ECO:0000305}.
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DR   EMBL; AF246294; AAF91326.1; -; Genomic_DNA.
DR   RefSeq; WP_000393901.1; NZ_WBPI01000006.1.
DR   AlphaFoldDB; Q9KI10; -.
DR   SMR; Q9KI10; -.
DR   STRING; 1396.DJ87_5652; -.
DR   TCDB; 2.A.37.2.2; the monovalent cation:proton antiporter-2 (cpa2) family.
DR   GeneID; 67506315; -.
DR   eggNOG; COG0475; Bacteria.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0015297; F:antiporter activity; IDA:UniProtKB.
DR   GO; GO:0015081; F:sodium ion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015385; F:sodium:proton antiporter activity; IDA:CACAO.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0009847; P:spore germination; IMP:UniProtKB.
DR   Gene3D; 1.20.1530.20; -; 1.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR004771; K/H_exchanger.
DR   InterPro; IPR038770; Na+/solute_symporter_sf.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   TIGRFAMs; TIGR00932; 2a37; 1.
PE   1: Evidence at protein level;
KW   Antiport; Germination; Ion transport; Membrane; Sodium; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..387
FT                   /note="Na(+)/H(+)-K(+) antiporter GerN"
FT                   /id="PRO_0000425690"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   387 AA;  41093 MW;  40DE45B71B715D01 CRC64;
     MEFEFFFQIA LILLSTKLAG DLSVRLGQPS VLGKLIVGIV IGPAVLGWIE NSELLTQLSN
     VGVILLMFMA GLETDLEELN ANRNSSLAVA LGGIILPFVG GYVSGLVMGM EQGNAVFLGL
     LLCATSVSIS VQTLRDLGKM KTRESTTMLG AAVFDDILVV ILLAFAMSFL GTDDVNLTMV
     ILKKVVFFAS IILIGWKGVP AIMRWLSPLR VSESIVSAAL IICFSFAYFG ELLGIAGIIG
     AFAAGIAISQ TNYKHEVEKK VEPIAYAMFV PVFFVSIGMN ITFDGIGNQI WFILALTVIA
     VLTKLIGCGF GARMTGFDAK SSAIIGAGMV SRGEVALIIA GTGLSSGLLA QDYFTAIVIV
     VILTTMITPP MLKYTFGAKD KAMKASK