SSUB_CORGL
ID SSUB_CORGL Reviewed; 243 AA.
AC Q8NR42; Q6M5W0;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Aliphatic sulfonates import ATP-binding protein SsuB {ECO:0000255|HAMAP-Rule:MF_01724};
DE EC=7.6.2.14 {ECO:0000255|HAMAP-Rule:MF_01724};
GN Name=ssuB {ECO:0000255|HAMAP-Rule:MF_01724};
GN OrderedLocusNames=Cgl1222, cg1379;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP FUNCTION IN ALIPHATIC SULFONATES TRANSPORT AND TAURINE TRANSPORT.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16204527; DOI=10.1128/aem.71.10.6104-6114.2005;
RA Koch D.J., Rueckert C., Rey D.A., Mix A., Puehler A., Kalinowski J.;
RT "Role of the ssu and seu genes of Corynebacterium glutamicum ATCC 13032 in
RT utilization of sulfonates and sulfonate esters as sulfur sources.";
RL Appl. Environ. Microbiol. 71:6104-6114(2005).
CC -!- FUNCTION: Part of the ABC transporter complex SsuABC involved in
CC aliphatic sulfonates import. Responsible for energy coupling to the
CC transport system (Probable). Is also involved in taurine transport.
CC Seems to not be involved in long chain aliphatic sulfonates transport
CC (chain length of eight carbon atoms or more). {ECO:0000255|HAMAP-
CC Rule:MF_01724, ECO:0000269|PubMed:16204527, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + aliphatic sulfonate-[sulfonate-binding
CC protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 +
CC [sulfonate-binding protein]Side 1.; EC=7.6.2.14;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01724};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (SsuB),
CC two transmembrane proteins (SsuC) and a solute-binding protein (SsuA).
CC {ECO:0000255|HAMAP-Rule:MF_01724}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01724};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01724}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Aliphatic
CC sulfonates importer (TC 3.A.1.17.2) family. {ECO:0000255|HAMAP-
CC Rule:MF_01724}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000036; BAB98615.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19926.1; -; Genomic_DNA.
DR RefSeq; NP_600446.1; NC_003450.3.
DR RefSeq; WP_011014212.1; NC_006958.1.
DR AlphaFoldDB; Q8NR42; -.
DR SMR; Q8NR42; -.
DR STRING; 196627.cg1379; -.
DR TCDB; 3.A.1.17.12; the atp-binding cassette (abc) superfamily.
DR KEGG; cgb:cg1379; -.
DR KEGG; cgl:Cgl1222; -.
DR PATRIC; fig|196627.13.peg.1202; -.
DR eggNOG; COG1116; Bacteria.
DR HOGENOM; CLU_000604_1_22_11; -.
DR OMA; HDMSLAR; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51291; SSUB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..243
FT /note="Aliphatic sulfonates import ATP-binding protein
FT SsuB"
FT /id="PRO_0000279910"
FT DOMAIN 11..230
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ SEQUENCE 243 AA; 25977 MW; EFD060BF8E5D7324 CRC64;
MTATLSLKPA ATVRGLRKSY GTKEVLQGID LTINCGEVTA LIGRSGSGKS TILRVLAGLS
KEHSGSVEIS GNPAVAFQEP RLLPWKTVLD NVTFGLNRTD ISWSEAQERA SALLAEVKLP
DSDAAWPLTL SGGQAQRVSL ARALISEPEL LLLDEPFGAL DALTRLTAQD LLLKTVNTRN
LGVLLVTHDV SEAIALADHV LLLDDGAITH SLTVDIPGDR RTHPSFASYT AQLLEWLEIT
TPA
