ID NHAA_BRUA2 Reviewed; 736 AA. AC Q2YMB3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 27-MAR-2024, entry version 96. DE RecName: Full=Na(+)/H(+) antiporter NhaA {ECO:0000255|HAMAP-Rule:MF_01844}; DE AltName: Full=Sodium/proton antiporter NhaA {ECO:0000255|HAMAP-Rule:MF_01844}; GN Name=nhaA {ECO:0000255|HAMAP-Rule:MF_01844}; GN OrderedLocusNames=BAB1_0425; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). CC -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for CC external protons. {ECO:0000255|HAMAP-Rule:MF_01844}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out); CC Xref=Rhea:RHEA:29251, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01844}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29252; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01844}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01844}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01844}. CC -!- SIMILARITY: In the N-terminal section; belongs to the NhaA Na(+)/H(+) CC (TC 2.A.33) antiporter family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase S49 CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAJ10381.1; Type=Erroneous initiation; Evidence={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; AM040264; CAJ10381.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_002971575.1; NZ_KN046823.1. DR AlphaFoldDB; Q2YMB3; -. DR SMR; Q2YMB3; -. DR STRING; 359391.BAB1_0425; -. DR GeneID; 3787184; -. DR KEGG; bmf:BAB1_0425; -. DR HOGENOM; CLU_020970_0_0_5; -. DR PhylomeDB; Q2YMB3; -. DR Proteomes; UP000002719; Chromosome I. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-UniRule. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR GO; GO:0006885; P:regulation of pH; IEA:InterPro. DR CDD; cd07023; S49_Sppa_N_C; 1. DR Gene3D; 6.20.330.10; -; 1. DR Gene3D; 1.20.1530.10; Na+/H+ antiporter like domain; 1. DR HAMAP; MF_01844; NhaA; 1. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR023171; Na/H_antiporter_dom_sf. DR InterPro; IPR004670; NhaA. DR InterPro; IPR002142; Peptidase_S49. DR InterPro; IPR047272; S49_SppA_C. DR NCBIfam; TIGR00773; NhaA; 1. DR PANTHER; PTHR30341:SF0; NA(+)_H(+) ANTIPORTER NHAA; 1. DR PANTHER; PTHR30341; SODIUM ION/PROTON ANTIPORTER NHAA-RELATED; 1. DR Pfam; PF06965; Na_H_antiport_1; 1. DR Pfam; PF01343; Peptidase_S49; 1. DR SUPFAM; SSF52096; ClpP/crotonase; 1. PE 3: Inferred from homology; KW Antiport; Cell inner membrane; Cell membrane; Ion transport; Membrane; KW Reference proteome; Sodium; Sodium transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..736 FT /note="Na(+)/H(+) antiporter NhaA" FT /id="PRO_0000334475" FT TRANSMEM 23..43 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 58..78 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 96..116 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 126..146 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 155..175 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 178..198 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 201..221 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 224..244 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 265..285 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 298..318 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 334..354 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT TRANSMEM 367..387 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01844" FT REGION 1..387 FT /note="Na(+)/H(+) antiporter NhaA" FT REGION 388..736 FT /note="Peptidase S49" SQ SEQUENCE 736 AA; 78587 MW; 7C5E5742B5EC5654 CRC64; MNHSPQSARP VSIMRRFLDS EAAGGITLMA AAALALIVAN SPFAQTYFDA LHLYIGPLSL AHWINDALMA IFFLLVGLEI KREMLDGQLA SWPNRMLPGI AAAGGVILPA IIFAVLNHDN PAKLRGWAVP SATDIAFALG VLSLLGSRAP SSLKVFLATL AILDDLAAVV IIAIFYTAEI SMPYLGAAFI TAAVLFVMNR MGVVKLLPYL ISAVILWFFV FNSGVHATVA GVVAALMIPL KPAPGRPDDM TSPLHKLEHA LAKPVAFIVV PIFGFANAGI SFKGLEASVL GDTLTLGILL GLFLGKQFGV FGAAWLAIKT GLAEKPMGAS WVQLYGVAIL CGIGFTMSIF IGLLSFPSDL MQTETKIGVL SGSALSAICG YLLLRAARPD QSAANPLWKA DESPEAKNFG RFLCVFHFAS YIASTYCTER LQAASSLLRR SSLEFALPGL LKRLIPRRFR AVETEIPVVR LHGAIMTGGT SLRPTLSLAS TAGILEKAFA DKHAPAVAIS INSPGGAPVQ SRLIYRRIRD LAVEHQKKVF VFVEDVAASG GYMIALAGDE IIADPSSIVG SIGVVSASFG FPELLKKIGV ERRVYTAGSN KVTLDPFQPE KAEDIERLKA LQLEIHATFI DMVKERRAGK LGDNPDLFSG LFWTGTTAAS LGLIDGLGDM RSFLRKTYGD KVKLKLIQPQ RGLLGRKLPG IGMDSGSVEP AQIAAHLGDG LLCVAEEKAI WARYGL //