KPSM1_ECOLX
ID KPSM1_ECOLX Reviewed; 258 AA.
AC P23889;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Polysialic acid transport protein KpsM;
GN Name=kpsM;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K1;
RX PubMed=1856162; DOI=10.1128/jb.173.15.4603-4610.1991;
RA Pavelka M.S. Jr., Wright L.F., Silver R.P.;
RT "Identification of two genes, kpsM and kpsT, in region 3 of the polysialic
RT acid gene cluster of Escherichia coli K1.";
RL J. Bacteriol. 173:4603-4610(1991).
RN [2]
RP TOPOLOGY.
RX PubMed=7715449; DOI=10.1111/j.1365-2958.1994.tb01323.x;
RA Pigeon R.P., Silver R.P.;
RT "Topological and mutational analysis of KpsM, the hydrophobic component of
RT the ABC-transporter involved in the export of polysialic acid in
RT Escherichia coli K1.";
RL Mol. Microbiol. 14:871-881(1994).
CC -!- FUNCTION: KpsM and KpsT constitute a system for the transport of
CC polysialic acid across the cytoplasmic membrane.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC {ECO:0000305}.
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DR EMBL; M57382; AAA24046.1; -; Genomic_DNA.
DR PIR; A42469; A42469.
DR RefSeq; WP_000124301.1; NZ_WVVR01000003.1.
DR AlphaFoldDB; P23889; -.
DR SMR; P23889; -.
DR OMA; AFRQVQP; -.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR000412; ABC_2_transport.
DR Pfam; PF01061; ABC2_membrane; 1.
DR PIRSF; PIRSF006648; DrrB; 1.
DR PRINTS; PR00164; ABC2TRNSPORT.
DR PROSITE; PS51012; ABC_TM2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..258
FT /note="Polysialic acid transport protein KpsM"
FT /id="PRO_0000182982"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:7715449"
FT TRANSMEM 31..54
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 55..61
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:7715449"
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 82..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:7715449"
FT TRANSMEM 109..132
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 133..143
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:7715449"
FT TRANSMEM 144..165
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 166..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:7715449"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 196..226
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:7715449"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 248..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:7715449"
FT DOMAIN 30..251
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
SQ SEQUENCE 258 AA; 29558 MW; D1F93E8BEB150389 CRC64;
MARSGFEVQK VTVEALFLRE IRTRFGKFRL GYLWAILEPS AHLLILLGIL GYVMHRTMPD
ISFPVFLLNG LIPFFIFSSI SKRSIGAIEA NQGLFNYRPV KPIDTIIARA LLETLIYVAV
YILLMLIVWM TGEYFEITNF LQLVLTWSLL IILSCGVGLI FMVVGKTFPE MQKVLPILLK
PLYFISCIMF PLHSIPKQYW SYLLWNPLVH VVELSREAVM PGYISEGVSL NYLAMFTLVT
LFIGLALYRT REEAMLTS
