ID   CARNT_ACIB2             Reviewed;         550 AA.
AC   D0C9N4;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Carnitine transporter {ECO:0000305};
GN   ORFNames=HMPREF0010_01347 {ECO:0000312|EMBL:EEX03953.1};
OS   Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG
OS   19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=575584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC   109757 / NCIMB 12457 / NCTC 12156 / 81;
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
RN   [2]
RP   FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC   109757 / NCIMB 12457 / NCTC 12156 / 81;
RX   PubMed=30318737; DOI=10.1002/mbo3.752;
RA   Breisch J., Waclawska I., Averhoff B.;
RT   "Identification and characterization of a carnitine transporter in
RT   Acinetobacter baumannii.";
RL   MicrobiologyOpen 7:E752-E752(2018).
CC   -!- FUNCTION: Catalyzes the energy-dependent uptake of carnitine and is
CC       essential for growth on carnitine. Can also mediate the uptake of
CC       choline. Is probably a proton:substrate symporter.
CC       {ECO:0000269|PubMed:30318737}.
CC   -!- ACTIVITY REGULATION: Inhibited by the protonophore 3,3',4',5-
CC       tetrachlorosalicylanilide (TCS). Not activated by osmolarity.
CC       {ECO:0000269|PubMed:30318737}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes growth on
CC       carnitine as sole carbon and energy source, but does not affect growth
CC       on acetate. {ECO:0000269|PubMed:30318737}.
CC   -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
CC       {ECO:0000305}.
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DR   EMBL; GG704573; EEX03953.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0C9N4; -.
DR   SMR; D0C9N4; -.
DR   EnsemblBacteria; EEX03953; EEX03953; HMPREF0010_01347.
DR   BioCyc; ABAU575584-HMP:GM69-1362-MON; -.
DR   Proteomes; UP000005740; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0071705; P:nitrogen compound transport; IEA:InterPro.
DR   InterPro; IPR000060; BCCT_transptr.
DR   PANTHER; PTHR30047; PTHR30047; 1.
DR   Pfam; PF02028; BCCT; 1.
DR   TIGRFAMs; TIGR00842; bcct; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..550
FT                   /note="Carnitine transporter"
FT                   /id="PRO_0000446221"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        477..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   550 AA;  60971 MW;  897EE43511BB75C7 CRC64;
     MDMDNQNTKI YTDKFLAVTS LLFVFISVAG LAIYSQESIK IAATWMQWTT SVFTTPVLLF
     AFLAIIFTFG LAFSKYGKIK LGEGKPQYST MSWIFMFILS GIGSSTLYWG FLDWAYYYQT
     PGLSLPPESA EALKYSVAYS FFHSGLSAWA IYALASISLC YSYHVRKNKG LSLASVIEAV
     TGFKSTGVVG RLVDLMFLLC MFGALTISLV LTAVTFTNIL SQLTGIPNTF MTKVIIILAV
     SVLFALSSYV GMDKGMQRLS HMVCLGVVLF AIYVLCFGPT QFILNNSLMS FGLMATNFVD
     MSLFTDPMGD GKFTREWTVF YWLWWISYAP GVALFVTRVS KGRTIKEVIF AMVIGGSVGL
     WFIFGVFENY SVYSFIHGAV NVPQILSQQG GEVAIGQLLS LLPAGKLMMW IFLGIMVVFL
     AAHMDAVGYA VSATCTRGLS EGQDPSPNAR LFWCVMLTLV PIAMIFSKAP LDTMKTATIV
     TALPFIVIIL IQTYGLVKWL IQDYAKVPSH LIEQQGYDDQ EIGLNQTQDE HAKRMQLELA
     SSIKLDRKTS