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Database: UniProt
Entry: A6VQK0_ACTSZ
LinkDB: A6VQK0_ACTSZ
Original site: A6VQK0_ACTSZ 
ID   A6VQK0_ACTSZ            Unreviewed;       330 AA.
AC   A6VQK0;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=D-galactose/methyl-galactoside binding periplasmic protein MglB {ECO:0000256|ARBA:ARBA00034344};
GN   OrderedLocusNames=Asuc_1898 {ECO:0000313|EMBL:ABR75247.1};
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR75247.1, ECO:0000313|Proteomes:UP000001114};
RN   [1] {ECO:0000313|Proteomes:UP000001114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC   {ECO:0000313|Proteomes:UP000001114};
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
CC   -!- SUBUNIT: The ABC transporter complex is composed of one ATP-binding
CC       protein (MglA), two transmembrane proteins (MglC) and a solute-binding
CC       protein (MglB). {ECO:0000256|ARBA:ARBA00034323}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC       {ECO:0000256|ARBA:ARBA00007639}.
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DR   EMBL; CP000746; ABR75247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VQK0; -.
DR   STRING; 339671.Asuc_1898; -.
DR   KEGG; asu:Asuc_1898; -.
DR   eggNOG; COG1879; Bacteria.
DR   HOGENOM; CLU_037628_3_1_6; -.
DR   OrthoDB; 9769193at2; -.
DR   Proteomes; UP000001114; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   CDD; cd01539; PBP1_GGBP; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   InterPro; IPR044085; MglB-like_PBP1.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR025997; SBP_2_dom.
DR   PANTHER; PTHR30036:SF2; D-GALACTOSE-BINDING PERIPLASMIC PROTEIN; 1.
DR   PANTHER; PTHR30036; D-XYLOSE-BINDING PERIPLASMIC PROTEIN; 1.
DR   Pfam; PF13407; Peripla_BP_4; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001114};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..330
FT                   /note="D-galactose/methyl-galactoside binding periplasmic
FT                   protein MglB"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002704204"
FT   DOMAIN          28..298
FT                   /note="Periplasmic binding protein"
FT                   /evidence="ECO:0000259|Pfam:PF13407"
SQ   SEQUENCE   330 AA;  35681 MW;  E2FB49A0F7D6EB0C CRC64;
     MKKLGLSAVA LAVGLVAGMS TAQAETKIGV TIYKYDDNFM ALMRKEINKE AEQLKDVRLL
     MNDSQNAQSI QNDQVDVLIS KGVKALAINL VDPSAAPTII GKAKPDDIPV VFFNKDPGEK
     ALAKYDKAYY VGTDPKESGL IQGDLIAKQW KANPALDLNK DGKIQYVLLK GEPGHPDAEA
     RTKYVIEKLN ELGIQTEQLF MDTGMWDAAM AKDKTDAWLS SARANEIEMI ISNNDGMAMG
     ALEAVKAHGK KLPIFGVDAL PEVLQLIKKG DIAGTVLNDG AGQGKAVVQL ANNLGQGKDA
     AEGTEWKVEN KVVRIPYVGV DKDNLSEFLK
//
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