KPST1_ECOLX
ID KPST1_ECOLX Reviewed; 219 AA.
AC P23888;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Polysialic acid transport ATP-binding protein KpsT;
GN Name=kpsT;
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 CHARACTERIZATION.
RX PubMed=8051103; DOI=10.1016/s0021-9258(17)32139-7;
RA Pavelka M.S. Jr., Hayes S.F., Silver R.P.;
RT "Characterization of KpsT, the ATP-binding component of the ABC-transporter
RT involved with the export of capsular polysialic acid in Escherichia coli
RT K1.";
RL J. Biol. Chem. 269:20149-20158(1994).
CC -!- FUNCTION: Putative ATP-binding protein, and an energy coupling
CC component for the transport of polysialic acid across the cytoplasmic
CC membrane.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; M57381; AAA24047.1; -; Genomic_DNA.
DR PIR; B42469; B42469.
DR RefSeq; WP_000590258.1; NZ_WVVR01000003.1.
DR AlphaFoldDB; P23888; -.
DR SMR; P23888; -.
DR PRIDE; P23888; -.
DR OMA; VHIVYRV; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03220; ABC_KpsT_Wzt; 1.
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; IPR015860; ABC_transpr_TagH-like.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Transport.
FT CHAIN 1..219
FT /note="Polysialic acid transport ATP-binding protein KpsT"
FT /id="PRO_0000092394"
FT DOMAIN 2..218
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 219 AA; 24939 MW; F1C8B5EE2BF0B2DA CRC64;
MIKIENLTKS YRTPTGRHYV FKNLNIIFPK GYNIALIGQN GAGKSTLLRI IGGIDRPDSG
NIITEHKISW PVGLAGGFQG SLTGRENVKF VARLYAKRDE LNERVDFVEE FSELGKYFDM
PIKTYSSGMR SRLAFGLSMA FKFDYYLIDE ITAVGDAKFK KKCSDIFDKI REKSHLIMVS
HSERALKEYC DVAIYLNKEG QGKFYKNVTE AIADYKKDL