ID A0A269VZA1_9BACL Unreviewed; 951 AA.
AC A0A269VZA1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Na+/H+ antiporter subunit A {ECO:0000313|EMBL:PAK50550.1};
GN ORFNames=CHH75_18050 {ECO:0000313|EMBL:PAK50550.1};
OS Paenibacillus sp. 7541.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2026236 {ECO:0000313|EMBL:PAK50550.1, ECO:0000313|Proteomes:UP000215741};
RN [1] {ECO:0000313|EMBL:PAK50550.1, ECO:0000313|Proteomes:UP000215741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7541 {ECO:0000313|EMBL:PAK50550.1,
RC ECO:0000313|Proteomes:UP000215741};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}.
CC -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit A
CC family. {ECO:0000256|ARBA:ARBA00008483}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAK50550.1}.
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DR EMBL; NQLZ01000029; PAK50550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A269VZA1; -.
DR Proteomes; UP000215741; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR007182; MnhB.
DR InterPro; IPR005663; MrpA/MnhA1/PhaAB.
DR InterPro; IPR025383; MrpA_C/MbhD.
DR InterPro; IPR046806; MrpA_C/MbhE.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR001516; Proton_antipo_N.
DR NCBIfam; TIGR00940; 2a6301s01; 1.
DR PANTHER; PTHR43373:SF1; ANTIPORTER SUBUNIT MNHA2-RELATED; 1.
DR PANTHER; PTHR43373; NA(+)/H(+) ANTIPORTER SUBUNIT; 1.
DR Pfam; PF13244; MbhD; 1.
DR Pfam; PF20501; MbhE; 1.
DR Pfam; PF04039; MnhB; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
PE 3: Inferred from homology;
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000215741};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 533..555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 596..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 774..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 817..837
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 849..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 879..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 922..944
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..113
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 129..426
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 638..702
FT /note="MrpA C-terminal/MbhD"
FT /evidence="ECO:0000259|Pfam:PF13244"
FT DOMAIN 715..792
FT /note="MrpA C-terminal/MbhE"
FT /evidence="ECO:0000259|Pfam:PF20501"
FT DOMAIN 818..942
FT /note="Na+/H+ antiporter MnhB subunit-related protein"
FT /evidence="ECO:0000259|Pfam:PF04039"
SQ SEQUENCE 951 AA; 104377 MW; 3A93C0A09707CC9E CRC64;
MSTLHFAVMA PFIAALVVLL IYKITRRIHT GWLILPVPVL LFVYFLGLIP SIQAGNPVHE
VLEWIPSLGI NFTVYLDGLS LIFTLLISGI GSLVVLYSIF YMDKNKEAVH RFYIYLLLFM
GAMLGVVLSD NLMVLYGFWE MTSISSFLLI AFWNHRDRSR YGALKSMLIT VFGGLAMLAG
FILLYVMAGT FSVREIISNL HTITDHALFI PAMILVLLGA FTKSAQFPFH IWLPDAMEAP
TPVSAYLHSA TMVKAGIYLV ARLSPVFAGH SLWFWLVSAT GLVTLIYASV RAIKQTDLKA
LLAFSTISQL GLIMSLLGLG SAAAYFSGSV DTLIYTKATT AAVFHLMNHA IFKGALFMVV
GIVDHETGTR DIRRLGGLMT LMPITFTVAV IGAFSMAGLP PFNGFLSKEM FFTAVLHAAS
MEFWNVETWG VLIPIVAWIA SVFTFVYSMI LVFRTFTGRL QSDKLEKQPH EAPIGMLIPP
VILASLAIVF GLFPNLLSYS LIEPAMASIH PSLLQPGGFN VKIEFWHGWT PEIFMTIAII
IVGTLLYFLH GKLAVLNTAL TRKLSLNHLY DWGLRSLEGG GRSVTKSYMT GSLRHYVLYI
FVFFIAVLGG SLLLTDHIRF DISEFAPMSI YEAAAVIGLV VPAIVLPFVR TRLMAIILTG
AIGYMVVLFF VLFRAPDLAL TQMIVETVSV MLFLLCFYHL PKLKREKVAM SLKWKNLLIS
AGAGAVVTLI ALAASSDRAF ESISEFFVKE SYTLAGGKNI VNVILVDFRG FDTMLEVMVL
GIAALGIFAL IKVDSGEGVL GKREAASDLH LPNSNDVILR TISRVVIFIV LAFSWYLFMA
GHNEPGGGFI GGLMTTAALV LLSMAYGMDM TKNIIPVSFR RMTAIGLMIA LLTGVGSFLF
GAPFLSHAFD YFDLPLLGET ELATAVLFDL GVYLAVVGVT MTIINSIGRD N
//
