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Database: UniProt
Entry: A0A0M2CWB7_9MICC
LinkDB: A0A0M2CWB7_9MICC
Original site: A0A0M2CWB7_9MICC 
ID   A0A0M2CWB7_9MICC        Unreviewed;      1036 AA.
AC   A0A0M2CWB7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Monovalent cation/H+ antiporter subunit A {ECO:0000313|EMBL:EYT53429.1};
GN   ORFNames=H488_0107030 {ECO:0000313|EMBL:EYT53429.1};
OS   Kocuria sp. UCD-OTCP.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT53429.1, ECO:0000313|Proteomes:UP000033173};
RN   [1] {ECO:0000313|EMBL:EYT53429.1, ECO:0000313|Proteomes:UP000033173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT53429.1,
RC   ECO:0000313|Proteomes:UP000033173};
RX   PubMed=23661474;
RA   Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT   "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:E00172-13(2013).
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   -!- 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:EYT53429.1}.
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DR   EMBL; AOSQ01000011; EYT53429.1; -; Genomic_DNA.
DR   RefSeq; WP_017832623.1; NZ_AOSQ01000011.1.
DR   AlphaFoldDB; A0A0M2CWB7; -.
DR   HOGENOM; CLU_007100_2_0_11; -.
DR   Proteomes; UP000033173; 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: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   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        75..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        103..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        368..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        503..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        575..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        610..627
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        634..653
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        659..678
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        699..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        755..774
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        840..862
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        868..888
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        900..925
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        945..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..100
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          126..401
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          619..682
FT                   /note="MrpA C-terminal/MbhD"
FT                   /evidence="ECO:0000259|Pfam:PF13244"
FT   DOMAIN          693..772
FT                   /note="MrpA C-terminal/MbhE"
FT                   /evidence="ECO:0000259|Pfam:PF20501"
FT   DOMAIN          841..963
FT                   /note="Na+/H+ antiporter MnhB subunit-related protein"
FT                   /evidence="ECO:0000259|Pfam:PF04039"
FT   REGION          999..1036
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1036 AA;  109751 MW;  B0949816EDCAC571 CRC64;
     MTAVLLLHAV VAAVAPLLFA RMGRSAFYLL AAVPFAGFLW LLGSGPRVYG PEGGWTEGGE
     WIPSLRLDLV LRMDALSWTM SLLVLGVGSL VLFYCARYFK SGASGIGGFG AQLLAFAGAM
     FGLVTADDML VLFVFWEITT VLSFLLISYS RTRLSARRAA LQALVLTTAG GLAMLVGIVM
     LGQAAGTYRI SEVLAAAPEL AQRGTVVDVA ILLLLVGAVT KSALIPLHFW LPAAMAAPTP
     VSAYLHAAAM VKAGIYLVAR FAPGFAETAL WQPTIAVLGL GTMLFGGWAA LKQYDLKLIL
     AYGTVSQLGF LMVIVGRGSA DTAQAGMAML LAHGLFKATL FLVVGIIDHR AGTRDIRRLS
     GLAGRVPVLF AVSLVAAASM AGLPPLAGFV AKEAVLTAFA HDVEGTAGTV VLAGLVVGSV
     LTFAYSARFV WGGFAHKSAE FSELDAGVGG RAVVSDMHRV EPAFLAAPLV LSVLTVVLGL
     WPQPVDAMLQ PYVDQFPAVE HDFYLALWHG FTPALGLSAL IVAGGILLHR FRSQVADLQR
     ALPSLPPGEL LYRRVVNVLD LAAVWITGRT QRGSLMFYLS VILITAIVVP LVALIAEETP
     PLGALRVSDG PGQLIAGVAM VVAALLVPLA RKRFLAVLLV SVTGYGLALI FALQGAPDLA
     LTQTLVETVL LVAFVLALRS LPAPLWHRNP AGRRLLRGTI AVTFGLFMMA LAAFSISSRT
     ADPISLELPR MAYELGDGQN VVNVILVDIR AWDTFGEISV LVLAATGVAS LIFVTGRGDR
     IVRSGDDPTT DQLRVIRRRN AAAVSPGGEP LEVGLARRDD DLEDPYLLAG RTMAPERRSI
     VFEVVTRLLF HTFMMVSLYL LIAGHNDPGG GFAGGLMAGL ALTVRYLAGG RYELELATPI
     NAGTMLGTGL ALAALYAVTP VFFGGSVMQS YTFEAELPLF GAEKFVTALI FDIAVYLIVV
     GLILDILRSL GGRIDQRIEE DAVRRRRRTP GRGTRIRVTR QRKVSAGAPA GATAAASATS
     PTAIARIRTD GGNEHR
//
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