ID A0A0Q5LWF1_9MICO Unreviewed; 435 AA.
AC A0A0Q5LWF1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Ion channel protein {ECO:0000313|EMBL:KQR54808.1};
GN ORFNames=ASF88_08705 {ECO:0000313|EMBL:KQR54808.1};
OS Leifsonia sp. Leaf336.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736341 {ECO:0000313|EMBL:KQR54808.1, ECO:0000313|Proteomes:UP000050966};
RN [1] {ECO:0000313|EMBL:KQR54808.1, ECO:0000313|Proteomes:UP000050966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR54808.1,
RC ECO:0000313|Proteomes:UP000050966};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR54808.1, ECO:0000313|Proteomes:UP000050966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR54808.1,
RC ECO:0000313|Proteomes:UP000050966};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000256|ARBA:ARBA00009476}.
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:KQR54808.1}.
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DR EMBL; LMOZ01000001; KQR54808.1; -; Genomic_DNA.
DR RefSeq; WP_055916415.1; NZ_LMOZ01000001.1.
DR AlphaFoldDB; A0A0Q5LWF1; -.
DR STRING; 1736341.ASF88_08705; -.
DR OrthoDB; 2729535at2; -.
DR Proteomes; UP000050966; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR CDD; cd00400; Voltage_gated_ClC; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR PANTHER; PTHR43427; CHLORIDE CHANNEL PROTEIN CLC-E; 1.
DR PANTHER; PTHR43427:SF9; ION-TRANSPORT PROTEIN YFEO-RELATED; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000050966};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 435 AA; 44150 MW; D56E20ACB7A47A04 CRC64;
MTSREPQPEL AAPSVRSLVL LSIPAVLIGV ISALTLWVVD EVAGVIDDGI WKSLPSALGI
DPSSGWWIFL ILTVTGLAVG LTVWLVPGHA GPDSATTELV TTPLRIGIVP SLALAAVLGL
AGGVSLGPEN PIIAINVSIL VALVGRIWKA VPSQLVMLMA ASGTIGALFG TPVAAALVFT
GIVAAVKGGG ALWDKLFLPL VSAAAGSLTM TLLAHPHLAI PMPAYTHVTG WDVLAALIIG
AVATGVGLLG AVLFPLIHRA FHALRQPVLI TLAGGIVLGL VGAVGGPITL FKGLEQMGTL
VVNRADYSIG QLVLIVVVKL VALLVAASSG FRGGRVFPAV FIGAALGTLT VALVPVVPLP
VAIAAAVMGI TLAVTRDGWI AIFVGVAVTQ NLLVLPILSL AVLPAWLMVT KAPEFLITPK
AITPTSPRAA DGAGR
//
