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 07-APR-2021, entry version 87. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB015981; BAA35095.1; -; Genomic_DNA. DR EMBL; DQ659238; ABG67110.1; -; Genomic_DNA. DR RefSeq; WP_042727539.1; NZ_UGZN01000001.1. 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:0015297; F:antiporter activity; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR GO; GO:0030004; P:cellular monovalent inorganic cation homeostasis; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW. DR InterPro; IPR025383; DUF4040. DR InterPro; IPR005663; MrpA/MnhA1/PhaAB. DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr. 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 PRINTS; PR01435; NPOXDRDTASE5. 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 //