MALF_VIBCH
ID MALF_VIBCH Reviewed; 524 AA.
AC Q9KL06; Q9L527;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalF {ECO:0000250|UniProtKB:P02916};
GN Name=malF; OrderedLocusNames=VC_A0944;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 232-524.
RC STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RA Dutta P.P., Roychoudhury S., Chaudhuri K.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the ABC transporter complex MalEFGK involved in
CC maltose/maltodextrin import. Probably responsible for the translocation
CC of the substrate across the membrane. {ECO:0000250|UniProtKB:P02916}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MalK),
CC two transmembrane proteins (MalG and MalF) and a solute-binding protein
CC (MalE). {ECO:0000250|UniProtKB:P02916}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P02916}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P02916}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. MalFG subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF70321.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003853; AAF96840.1; -; Genomic_DNA.
DR EMBL; AF260245; AAF70321.1; ALT_INIT; Genomic_DNA.
DR PIR; G82397; G82397.
DR RefSeq; NP_233328.1; NC_002506.1.
DR RefSeq; WP_010895488.1; NC_002506.1.
DR AlphaFoldDB; Q9KL06; -.
DR SMR; Q9KL06; -.
DR STRING; 243277.VC_A0944; -.
DR DNASU; 2612560; -.
DR EnsemblBacteria; AAF96840; AAF96840; VC_A0944.
DR KEGG; vch:VC_A0944; -.
DR PATRIC; fig|243277.26.peg.3556; -.
DR eggNOG; COG1175; Bacteria.
DR HOGENOM; CLU_016047_20_0_6; -.
DR OMA; DGHNSTK; -.
DR BioCyc; VCHO:VCA0944-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:1990060; C:maltose transport complex; IBA:GO_Central.
DR GO; GO:0015423; F:ABC-type maltose transporter activity; IBA:GO_Central.
DR GO; GO:0042956; P:maltodextrin transmembrane transport; IBA:GO_Central.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR Gene3D; 1.20.58.370; -; 1.
DR InterPro; IPR030156; MalF-like.
DR InterPro; IPR035277; MalF_N.
DR InterPro; IPR029345; MalF_P2.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR47314:SF1; PTHR47314:SF1; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF14785; MalF_P2; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..524
FT /note="Maltose/maltodextrin transport system permease
FT protein MalF"
FT /id="PRO_0000060076"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 46..49
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..69
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 70..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..104
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 105..289
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..312
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 313..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 348..379
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..402
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 403..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..458
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 459..493
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..516
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 517..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 291..515
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 524 AA; 57970 MW; B041619A3F2734E2 CRC64;
MQSVQGTQAM SDPTAVRPAD KRAFLKWAVL GAVGIVNGYA TILMYSRGEV AFALLTLILT
TLALYIFGSR KTYAHRYIYP GIAGMILFIL FPLAYTVGLA FTNYSAKNQL TLERAQSVLM
DQTFQSGESY AFQLYKTEQG YRLLIEDGDE RLATAPFSLS GNVPTDLNLE VIGGIDGEVE
PIKTIIGYRT ELSGIDLHFP DGEDIRMSGL RKFAAVKPLY TLQDDGETLT NNQSGQVLRP
NMEIGFYQPI NESGEFVGER VSPGFVVSIG THNFERVWKD EGIKEPFINI FIWTVIFSVL
TVIFTLMIGL VLASVVQWEA LKGRAVYRVL LILPYAVPAF ISILIFRGLF NQSFGEINMV
LNGLFGLSPA WFSDPLLAKT MVLIVNTWLG FPYMMIFCMG LLKAIPDDLY EASAIDGANF
IHNFTKITLP MMIKPLTPLL IASFAFNFNN FVMIQLLTQG GPNRIGTSEP AGYTDLLVSY
TYRIAFEGTG GQDFGLASAI ATLIFLLVGA LALLNLRFTK LSQQ
