MDTB_SERP5
ID MDTB_SERP5 Reviewed; 1039 AA.
AC A8GHQ9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Multidrug resistance protein MdtB {ECO:0000255|HAMAP-Rule:MF_01423};
DE AltName: Full=Multidrug transporter MdtB {ECO:0000255|HAMAP-Rule:MF_01423};
GN Name=mdtB {ECO:0000255|HAMAP-Rule:MF_01423}; OrderedLocusNames=Spro_3553;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Part of a tripartite efflux system composed of MdtA, MdtB and
CC MdtC. MdtB forms a heteromultimer with MdtC. {ECO:0000255|HAMAP-
CC Rule:MF_01423}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01423}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01423}.
CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. MdtB subfamily. {ECO:0000255|HAMAP-Rule:MF_01423}.
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DR EMBL; CP000826; ABV42649.1; -; Genomic_DNA.
DR RefSeq; WP_012146262.1; NC_009832.1.
DR AlphaFoldDB; A8GHQ9; -.
DR SMR; A8GHQ9; -.
DR STRING; 399741.Spro_3553; -.
DR EnsemblBacteria; ABV42649; ABV42649; Spro_3553.
DR KEGG; spe:Spro_3553; -.
DR eggNOG; COG0841; Bacteria.
DR HOGENOM; CLU_002755_1_2_6; -.
DR OMA; FIIPCFY; -.
DR OrthoDB; 145346at2; -.
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:UniProtKB-UniRule.
DR Gene3D; 3.30.2090.10; -; 2.
DR HAMAP; MF_01423; MdtB; 1.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR022831; Multidrug-R_MdtB.
DR PANTHER; PTHR32063; PTHR32063; 1.
DR Pfam; PF00873; ACR_tran; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82714; SSF82714; 2.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1039
FT /note="Multidrug resistance protein MdtB"
FT /id="PRO_1000068505"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 863..883
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 888..908
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 968..988
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
SQ SEQUENCE 1039 AA; 111988 MW; 3617E66C89F202D1 CRC64;
MQVMPPNPGG GPSRLFILRP VATTLLMVAI LLAGIIGYRA LPVSALPEVD YPTIQVVTLY
PGASPDVVTS AITAPLERQF GQMSGLKQMA SQSSGGASVV TLQFQLELPL DVAEQEVQAA
INSATNLLPS DLPYPPIYSK VNPADPPILT LAVTSSAMPM TQVEDMVETR VAQKISQVTG
VGLVTISGGQ RPAVRVKLNA AAVAAYGLDS ETIRTAISNA NVNSAKGSLD GPTRSVTLSA
NDQMKSADDY RQLIVAYQNG AAIRLQDIAT IEQGAENTRL AAWANKQPAI VLNIQRQPGV
NVITTADSIR EMLPQLIKSL PKSVDVKVLT DRTTTIRASV SDVQFELLLA VALVVMVIYV
FLRNVPATII PSVAVPLSLI GTFAAMYFLG FSINNLTLMA LTIATGFVVD DAIVVIENIS
RYIEKGEKPL DAALKGAGEI GFTIISLTFS LVAVLIPLLF MGDIVGRLFR EFAVTLAVAI
LISAVVSLTL TPMMCARMLS HESLRKQNRF SAASERFFDR VIARYGKWLK TVLNHPWLTL
GVAFSTLLLT VLLYLLIPKG FFPVQDNGII QGTLEAPQSV SFSNMAERQQ QVAAEILKDP
AVESLTSFVG VDGTNATLNS GRLQINLKPL SERSERIPAI ITRLQQMSTQ FPGVKLYLQP
VQDLTIDTQV SRTQYQFTLQ AMSLDDLSLW VPKLMAELQQ TPQLADVTSN WQDQGLVAYV
NVDRDSASRL GISMSDVDNA LYNAFGQRLI STIYTQANQY RVVLEHDVST TPGLAALNDI
RLTSSNGTIV PLSTIAKIEQ RFGPLSVNHL DQFPAATISF NVAGNYSLGE AVDAITLAEK
NLNLPKDITT QFQGATLAFQ AALGGTLWLI LAAVVAMYIV LGVLYESFIH PVTILSTLPT
AGVGALLALM MAGSELDVIA IIGIILLIGI VKKNAIMMID FALAAEREQG MTPYDAIYQA
CLLRFRPILM TTLAALLGAL PLMLSTGVGA ELRHPLGVCM VGGLVMSQIL TLFTTPVIYL
LFDKLARNTR RQPDAQELP