ID A0A0A0DE47_9STRE Unreviewed; 517 AA.
AC A0A0A0DE47;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Voltage-gated chloride channel family protein {ECO:0000313|EMBL:KGM36976.1};
GN ORFNames=SSIN_1277 {ECO:0000313|EMBL:KGM36976.1};
OS Streptococcus sinensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=176090 {ECO:0000313|EMBL:KGM36976.1, ECO:0000313|Proteomes:UP000030019};
RN [1] {ECO:0000313|EMBL:KGM36976.1, ECO:0000313|Proteomes:UP000030019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKU4 {ECO:0000313|EMBL:KGM36976.1,
RC ECO:0000313|Proteomes:UP000030019};
RA Teng J.L., Huang Y., Tse H., Lau S.K., Woo P.C.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KGM36976.1}.
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DR EMBL; JPEN01000070; KGM36976.1; -; Genomic_DNA.
DR RefSeq; WP_037616972.1; NZ_JPEN01000070.1.
DR AlphaFoldDB; A0A0A0DE47; -.
DR STRING; 176090.SSIN_1277; -.
DR PATRIC; fig|176090.4.peg.1238; -.
DR eggNOG; COG0038; Bacteria.
DR Proteomes; UP000030019; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR CDD; cd01031; EriC; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR Gene3D; 3.30.70.1450; Regulator of K+ conductance, C-terminal domain; 1.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR PANTHER; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45711:SF6; CHLORIDE CHANNEL PROTEIN; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR SUPFAM; SSF116726; TrkA C-terminal domain-like; 1.
DR PROSITE; PS51202; RCK_C; 1.
PE 4: Predicted;
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 436..517
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
SQ SEQUENCE 517 AA; 56970 MW; CB14461B96E0A89B CRC64;
MIRQTEQVSD TRKEFKFMSS SIISQVFRGI LVGIFAGVVV GAFRFLIEKS FHLVQAAYVR
GRSEWLWLVA LLFLYAFIVF INARLVRTER DIKGSGIPQV EAELKGLMSL SWWSILWKKF
LVGTLAISSG LMLGREGPSI QLGAMSGKGI SKWLKLSPLE ERALIASGAA AGLAAAFNAP
IAGLLFVVEE VYHHFSRVFW VSTLAASLVA NFISLSMFGL TPVLDMPDNI PFMGLEQYWI
YILMGLFLGL SGFLYEKAVL NIHLVYEALG KFFRLPKNYY PIFAFVLIIP IGYFLPHLLG
GGNQLILSLT SAHYTVGTLI LFFLLRFVWS MISYGSGLPG GIFLPILALG SLLGAAIGAL
CVQAGFISQE QFPIFIILGM SGYFGAISKA PLTAMILVTE MVGDIRNLMP LGLVTLMAYI
AMDLLKGAPV YEAMLEKMLP HRIEDDGETT LIEIPVSEKI AGRQVHELEL PHGVLITMNI
HKGKTQTVNG ASRLYLGDTI YVVVKKTEIG QIKDILL
//