ID F8DXQ2_CORRG Unreviewed; 1081 AA.
AC F8DXQ2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Multicomponent Na+:H+ antiporter subunit A/B {ECO:0000313|EMBL:AEI10389.1};
DE EC=1.6.5.3 {ECO:0000313|EMBL:AEI10389.1};
GN Name=mnhB {ECO:0000313|EMBL:AEI10389.1};
GN OrderedLocusNames=CRES_2036 {ECO:0000313|EMBL:AEI10389.1};
OS Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026 / SICGH
OS 158).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI10389.1, ECO:0000313|Proteomes:UP000000492};
RN [1] {ECO:0000313|EMBL:AEI10389.1, ECO:0000313|Proteomes:UP000000492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45100 / JCM 12819 / GTC 2026 / SICGH 158
RC {ECO:0000313|Proteomes:UP000000492};
RX PubMed=22524407; DOI=10.1186/1471-2164-13-141;
RA Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S.,
RA Schneider J., Trost E., Tauch A.;
RT "Complete genome sequence, lifestyle, and multi-drug resistance of the
RT human pathogen Corynebacterium resistens DSM 45100 isolated from blood
RT samples of a leukemia patient.";
RL BMC Genomics 13:141-141(2012).
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}.
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DR EMBL; CP002857; AEI10389.1; -; Genomic_DNA.
DR RefSeq; WP_013889371.1; NC_015673.1.
DR AlphaFoldDB; F8DXQ2; -.
DR STRING; 662755.CRES_2036; -.
DR KEGG; crd:CRES_2036; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_2_0_11; -.
DR Proteomes; UP000000492; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR007182; MnhB.
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 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 4: Predicted;
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:AEI10389.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000492};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 30..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 591..612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 632..648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 655..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 716..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 775..792
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 847..866
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 872..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 902..923
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 943..962
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..137
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 153..426
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 637..701
FT /note="MrpA C-terminal/MbhD"
FT /evidence="ECO:0000259|Pfam:PF13244"
FT DOMAIN 714..788
FT /note="MrpA C-terminal/MbhE"
FT /evidence="ECO:0000259|Pfam:PF20501"
FT DOMAIN 843..959
FT /note="Na+/H+ antiporter MnhB subunit-related protein"
FT /evidence="ECO:0000259|Pfam:PF04039"
FT REGION 971..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1081 AA; 115609 MW; BE9924BFC3391A4F CRC64;
MAILAIPAVL LIALACVPLL VKILDRNAGW PLALAFLSLA GFLISQAKDV LHGSGIFWTH
SWIKGFLSGS TAQNPAELTS VPENISYNTA FSGDMQIALR LDALSLAFTL LALIIGAVVF
IYSTRYLHRG TKILSFYSLM TTFMLAVVVL FLADDVVLLF IGWELVSLAS FFLIARAGSS
GEAGSIRTLL LTFTGGLFLV AALAVMVATT GTMSVTEIIA SPRWEEEPVR IGLVAILIAL
AAFSKAAQIP FHFWLPEAMA ADTPVSAFLH AAAVVKAGIF LLLRFNALFK GVAMWHYVLI
VVGMTTAVMA AVFAMQKTDL KKLTAYSTVS QLGWIVATIG VGTPFAISAA IAHTAAHALF
KSSLFMLVGV VDHQAGSRDI RRLGPLWRQM PLTFGSAVIA AASMAAIPPT FGFVSKEGML
EAFTEAPFNS IGVGLLLFVA GVGALATLLY SARYVFGAFI DGKRDMSHVK EAQLSLLLPA
ALPGVLSLPL VLFMSSANHP IDAVVEATGA GEAHTHLALW HGVTLPLVIS LIVMAVGLVA
ILNRRRVFDP LEDRRLGLIA GEDIIQKVED LSTRLGKILA RPAASIAPSR HVVWILSMII
LLAAFAVMGP GRLEGITALA PRISGIDRPE DLIGLIIVAA ATISLTATRS RFASVVLVGV
IGAGVSWVML TLGAPDVAQT QLLVEFCVVV IMMLVIRHQP RLYLREGENR TKFATTLAVI
MGLITFFGVW LLIGRHDKPQ IAQWYLENTP DISGANNVVA AILVEFRAFD TMGELIVLGM
AGIVIAAIIG SIPRSPFPGY GPGSTAELFR APGSHRFPDV HKVPELAPFY SKYLRSTYLN
SIISRMALRP LLPVLIILSA VVFWRGHQAP GGGFLAALIA ACALFYLYLG RASARKLGSD
ELGYRLVGSG ILLALLTGMA GFFEGSFLAP LHTEIAGVHL TTSLLFDGGV YLAVIGLIVI
VINQMGGRER PGVNPSDMPF GRRQATFSPK LSSLKNSREH HPVEGKRADN AKKISPVAVH
VGGSHITLNP SEVRKHAEDE RRSESGPRAG SESARAGVDN KKKPPKNQKK TSNDEEGDSE
K
//
