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Database: UniProt
Entry: A0A1Q9JSQ4_9FIRM
LinkDB: A0A1Q9JSQ4_9FIRM
Original site: A0A1Q9JSQ4_9FIRM 
ID   A0A1Q9JSQ4_9FIRM        Unreviewed;       260 AA.
AC   A0A1Q9JSQ4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Transport permease protein {ECO:0000256|RuleBase:RU361157};
GN   ORFNames=BHF70_06145 {ECO:0000313|EMBL:OLR59240.1};
OS   Anaerostipes sp. 494a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=1261636 {ECO:0000313|EMBL:OLR59240.1, ECO:0000313|Proteomes:UP000242190};
RN   [1] {ECO:0000313|EMBL:OLR59240.1, ECO:0000313|Proteomes:UP000242190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=494a {ECO:0000313|EMBL:OLR59240.1,
RC   ECO:0000313|Proteomes:UP000242190};
RX   PubMed=27613689;
RA   Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT   "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT   Transferases and Their Diversity in the Proximal Colon of Swine.";
RL   Appl. Environ. Microbiol. 82:6788-6798(2016).
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}.
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:OLR59240.1}.
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DR   EMBL; MJIF01000001; OLR59240.1; -; Genomic_DNA.
DR   RefSeq; WP_075759442.1; NZ_MJIF01000001.1.
DR   AlphaFoldDB; A0A1Q9JSQ4; -.
DR   STRING; 1261636.BHF70_06145; -.
DR   OrthoDB; 9786910at2; -.
DR   Proteomes; UP000242190; Unassembled WGS sequence.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR047817; ABC2_TM_bact-type.
DR   InterPro; IPR000412; ABC_2_transport.
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   PRINTS; PR00164; ABC2TRNSPORT.
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:UP000242190};
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        31..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361157"
FT   TRANSMEM        63..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361157"
FT   TRANSMEM        103..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361157"
FT   TRANSMEM        138..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361157"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361157"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361157"
FT   DOMAIN          32..252
FT                   /note="ABC transmembrane type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51012"
SQ   SEQUENCE   260 AA;  29908 MW;  AB4FA4752178891D CRC64;
     MKTYIENFKK YRFLLVELVK KGVKLKYRRS YLGILWTLLE PMLTTMVLTL VFGSMFGNPD
     PKFPVYILTG RLLYSFFSTA TNGAMKSIRT NAGMIKKVYV PKYIYPLSSV LFNFIIFALS
     LIVLVGACIV FKVYPNIYIL QAVVPILLLL LTAFGVGMIL STMAVFFRDL EYLWSVALMM
     IMYASAIFYP AERLLSKPGI YGYVLKVNPL YLLIHNFRQA IYGRPMNMHF LAASFVFAVV
     TCIVGLVFFY KKQDEFILYI
//
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