OPUCA_LISMN
ID OPUCA_LISMN Reviewed; 397 AA.
AC Q9KHT9;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Carnitine transport ATP-binding protein OpuCA;
DE EC=7.6.2.9;
GN Name=opuCA;
OS Listeria monocytogenes.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1639;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=EGD / Serotype 1/2a;
RX PubMed=11055912; DOI=10.1128/aem.66.11.4696-4704.2000;
RA Fraser K.R., Harvie D., Coote P.J., O'Byrne C.P.;
RT "Identification and characterization of an ATP binding cassette L-carnitine
RT transporter in Listeria monocytogenes.";
RL Appl. Environ. Microbiol. 66:4696-4704(2000).
CC -!- FUNCTION: Part of the ABC transporter complex OpuCABCD involved in
CC carnitine uptake. Probably responsible for energy coupling to the
CC transport system. Involved, with BetL and GbuABC, in osmoprotection and
CC cryoprotection of Listeria. {ECO:0000269|PubMed:11055912}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + quaternary ammonium(out) = ADP + H(+) + phosphate
CC + quaternary ammonium(in); Xref=Rhea:RHEA:11036, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:35267,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.6.2.9;
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (OpuCA),
CC two transmembrane proteins (OpuCB and OpuCD) and a solute-binding
CC protein (OpuCC). {ECO:0000305|PubMed:11055912}.
CC -!- DISRUPTION PHENOTYPE: Mutants are impaired for growth at high
CC osmolarity in brain heart infusion broth, fail to grow in a defined
CC medium and show no detectable carnitine uptake.
CC {ECO:0000269|PubMed:11055912}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AF249729; AAF91339.1; -; Genomic_DNA.
DR PIR; AD1253; AD1253.
DR RefSeq; WP_003721933.1; NZ_VTKA01000001.1.
DR PDB; 5KS7; X-ray; 2.90 A; A/B=247-372.
DR PDBsum; 5KS7; -.
DR AlphaFoldDB; Q9KHT9; -.
DR SMR; Q9KHT9; -.
DR STRING; 1027396.LMOSA_23490; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG1125; Bacteria.
DR OMA; MYEFNRA; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0015418; F:ABC-type quaternary ammonium compound transporting activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031460; P:glycine betaine transport; IEA:InterPro.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005892; Gly-betaine_transp_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF00571; CBS; 2.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR01186; proV; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; CBS domain; Nucleotide-binding; Repeat;
KW Stress response; Translocase; Transport.
FT CHAIN 1..397
FT /note="Carnitine transport ATP-binding protein OpuCA"
FT /id="PRO_0000418132"
FT DOMAIN 2..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 255..311
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 315..373
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 377..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:5KS7"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:5KS7"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:5KS7"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:5KS7"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:5KS7"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:5KS7"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:5KS7"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:5KS7"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:5KS7"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:5KS7"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:5KS7"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:5KS7"
SQ SEQUENCE 397 AA; 45209 MW; 134CF427650AC83B CRC64;
MLKFEHVTKT YKGGKKAVND LTLNIDKGEF VCFIGPSGCG KTTTMKMINR LIEPTEGKIF
INDKDIMAED PVKLRRSIGY VIQQIGLMPH MTIRENIVLV PKLLKWSEEK KQERAKELIK
LVDLPEEFLD RYPYELSGGQ QQRIGVLRAL AAEQNLILMD EPFGALDPIT RDSLQEEFKN
LQKELGKTII FVTHDMDEAI KLADRIVIMK DGEIVQFDTP DEILRNPANS FVEDFIGKDR
LIEAKPDVTQ VAQIMNTNPV SITADKSLQA AITVMKEKRV DTLLVVDEGN VLKGFIDVEQ
IDLNRRTATS VMDIIEKNVF YVYEDTLLRD TVQRILKRGY KYIPVVDKDK RLVGIVTRAS
LVDIVYDSIW GTLEDATENQ EEQADSKTTE PEMKQEG
