ID C7M106_ACIFD Unreviewed; 316 AA.
AC C7M106;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Transport permease protein {ECO:0000256|RuleBase:RU361157};
GN OrderedLocusNames=Afer_1748 {ECO:0000313|EMBL:ACU54664.1};
OS Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC 103882 /
OS ICP).
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidimicrobium.
OX NCBI_TaxID=525909 {ECO:0000313|EMBL:ACU54664.1, ECO:0000313|Proteomes:UP000000771};
RN [1] {ECO:0000313|EMBL:ACU54664.1, ECO:0000313|Proteomes:UP000000771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP
RC {ECO:0000313|Proteomes:UP000000771};
RX PubMed=21304635; DOI=10.4056/sigs.1463;
RA Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Acidimicrobium ferrooxidans type strain
RT (ICP).";
RL Stand. Genomic Sci. 1:38-45(2009).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU361157};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU361157}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC {ECO:0000256|ARBA:ARBA00007783, ECO:0000256|RuleBase:RU361157}.
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DR EMBL; CP001631; ACU54664.1; -; Genomic_DNA.
DR AlphaFoldDB; C7M106; -.
DR STRING; 525909.Afer_1748; -.
DR KEGG; afo:Afer_1748; -.
DR eggNOG; COG1682; Bacteria.
DR HOGENOM; CLU_060703_3_0_11; -.
DR Proteomes; UP000000771; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR047817; ABC2_TM_bact-type.
DR PANTHER; PTHR30413:SF10; CAPSULE POLYSACCHARIDE EXPORT INNER-MEMBRANE PROTEIN CTRC; 1.
DR PANTHER; PTHR30413; INNER MEMBRANE TRANSPORT PERMEASE; 1.
DR Pfam; PF01061; ABC2_membrane; 1.
DR PROSITE; PS51012; ABC_TM2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU361157};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361157};
KW Reference proteome {ECO:0000313|Proteomes:UP000000771};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361157};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361157}; Transport {ECO:0000256|RuleBase:RU361157}.
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 136..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 171..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 236..253
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 282..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT DOMAIN 64..308
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000259|PROSITE:PS51012"
SQ SEQUENCE 316 AA; 35196 MW; EEF9F00DDF109205 CRC64;
MDTHLPASQP GDTKRYDPNR ALAIRLVRPR VSVTERLANI WRYRDLLRGL IVKEIRVKYK
DSFLGFLWSL VNPAMFILIY YIVFQKVLGS GIPLFAIFLA TGLLCWNLFQ TGIMGATGAV
VDNAGLVKKV AFPREILALA SVGSASVFFV FQAVVLAVFL VVFQVVPSVS YLWVALIGLV
ALLVFASGLG ILVSGITVYL RDVRHLMEIL LQAWFWATPV VYAFELVANK FADHHIPVWV
YLLNPVTPVV LAFQRTFYAK TDPYSVASHT VVQILPTAGP MWYFWGVLGV LVAGVVLFVV
ALWAFGRLEG NFAEEL
//
