MNHA1_STAAU
ID MNHA1_STAAU Reviewed; 801 AA.
AC Q9ZNG6; Q0Q2K7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Na(+)/H(+) antiporter subunit A1;
DE AltName: Full=Mnh complex subunit A1;
DE AltName: Full=Mrp complex subunit A1;
GN Name=mnhA1; Synonyms=mrpA1;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF ANTIPORTER
RP ACTIVITY.
RC STRAIN=ATCC 21027 / 209-P;
RX PubMed=9852009; DOI=10.1128/jb.180.24.6642-6648.1998;
RA Hiramatsu T., Kodama K., Kuroda T., Mizushima T., Tsuchiya T.;
RT "A putative multisubunit Na+/H+ antiporter from Staphylococcus aureus.";
RL J. Bacteriol. 180:6642-6648(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-801, CHARACTERIZATION, AND PROBABLE
RP ELECTROGENIC ANTIPORTER ACTIVITY.
RC STRAIN=RF4220;
RX PubMed=17293423; DOI=10.1128/jb.00021-07;
RA Swartz T.H., Ito M., Ohira T., Natsui S., Hicks D.B., Krulwich T.A.;
RT "Catalytic properties of Staphylococcus aureus and Bacillus members of the
RT secondary cation/proton antiporter-3 (Mrp) family are revealed by an
RT optimized assay in an Escherichia coli host.";
RL J. Bacteriol. 189:3081-3090(2007).
CC -!- FUNCTION: Mnh complex is a Na(+)Li(+)/H(+) antiporter involved in Na(+)
CC and/or Li(+) excretion. Na(+)/H(+) antiport consumes a transmembrane
CC electrical potential, and is thus inferred to be electrogenic. Does not
CC transport K(+), Ca(2+) or Mg(2+).
CC -!- ACTIVITY REGULATION: Na(+) extrusion is completely inhibited by the
CC H(+) conductor carbonyl cyanide m-chlorophenylhydrazone (CCCP).
CC -!- SUBUNIT: May form a heterooligomeric complex that consists of seven
CC subunits: mnhA1, mnhB1, mnhC1, mnhD1, mnhE1, mnhF1 and mnhG1.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit A
CC family. {ECO:0000305}.
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DR EMBL; AB015981; BAA35095.1; -; Genomic_DNA.
DR EMBL; DQ659238; ABG67110.1; -; Genomic_DNA.
DR RefSeq; WP_042727539.1; NZ_UGZN01000001.1.
DR AlphaFoldDB; Q9ZNG6; -.
DR SMR; Q9ZNG6; -.
DR TCDB; 2.A.63.1.3; the monovalent cation (k(+) or na(+)):proton antiporter-3 (cpa3) family.
DR PATRIC; fig|1280.3363.peg.306; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005451; F:monovalent cation:proton antiporter activity; IEA:InterPro.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR025383; MbhD-like_TM.
DR InterPro; IPR005663; MrpA/MnhA1/PhaAB.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR001516; Proton_antipo_N.
DR Pfam; PF13244; DUF4040; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR TIGRFAMs; TIGR00940; 2a6301s01; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Hydrogen ion transport; Ion transport; Membrane;
KW Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..801
FT /note="Na(+)/H(+) antiporter subunit A1"
FT /id="PRO_0000217071"
FT TRANSMEM 4..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 589..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..784
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 801 AA; 89386 MW; 2EEC9AED745917AC CRC64;
MSLLHIAVIL PLIFALIIPI LYRFFKRIHL GWFVLSVPIV IFIYMLTLIK TTMSGNTVMK
TLNWMPHFGM NFDLYLDGLG LLFSLLISGI GSLVVLYSIG YLSKSEQLGN FYCYLLLFMG
AMLGVVLSDN VIILYLFWEL TSFSSFLLIS FWRERQASIY GAQKSLIITV FGGLSLLGGI
ILLAIPTQSF SIQYMIQHAS EIQNSPFFIF AMILIMIGAF TKSAQFPFYI WLPDAMEAPT
PVSAYLHSAT MVKAGLYLIA RMTPIFAASQ GWVWTVTLVG LITLFWASLN ATKQQDLKGI
LAFSTVSQLG MIMAMLGIGA ISYHYQGDDS KIYAAAFTAA IFHLINHATF KGALFMITGA
VDHSTGTRDV KKLGGLLTIM PISFTITVIT ALSMAGVPPF NGFLSKESFL ETTFTASQAN
LFSVDTLGYL FPIIGIVGSV FTFVYSIKFI MHIFFGQYKP EQLPKKAHEV SILMLLSPAI
LATLVIVFGL FPGILTNSII EPATSSINHT VIDDVEFHMF HGLTPAFLST LVIYILGILL
IVTFSYWVKL LQRQPGKLTF NYWYNRSANV IPNYSEKMTN SYVTDYSRNN LVIIFGALIL
LTFVTIFSVP FNINFKDVSP IRIFEVCIVI LLLSAAFLIL FAKSRLFSII MLSAVGYAVS
VLFIFFKAPD LALTQFVVES ISTALFLLCF YHLPNLNRYN EKRSFQLTNA LIAGGVGLSV
IIIGLIAYGN RHFESISKFY QEHVYDLAHG KNMVNVILVD FRGMDTLFES SVLGIAGLAV
YTMIKLRKKR QTQGNEVKNH E
