IBPB_HISS2
ID IBPB_HISS2 Reviewed; 586 AA.
AC B0UUL1; Q7WZI4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Outer membrane transporter protein IbpB;
DE AltName: Full=TpsB transporter;
DE Flags: Precursor;
GN Name=ibpB; OrderedLocusNames=HSM_1490;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=16169703; DOI=10.1016/j.micpath.2005.08.002;
RA Tagawa Y., Sanders J.D., Uchida I., Bastida-Corcuera F.D., Kawashima K.,
RA Corbeil L.B.;
RT "Genetic and functional analysis of Haemophilus somnus high molecular
RT weight-immunoglobulin binding proteins.";
RL Microb. Pathog. 39:159-170(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possible member (with IbpA) of a two partner secretion
CC pathway (TPS) in which it would mediate the secretion of protein IbpA
CC (high molecular weight immunoglobulin-binding protein).
CC {ECO:0000269|PubMed:16169703}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}.
CC -!- DOMAIN: Probably a beta-barrel protein. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPS (TC 1.B.20) family. {ECO:0000305}.
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DR EMBL; AB087258; BAC78648.1; -; Genomic_DNA.
DR EMBL; CP000947; ACA31241.1; -; Genomic_DNA.
DR RefSeq; WP_012340629.1; NC_010519.1.
DR AlphaFoldDB; B0UUL1; -.
DR SMR; B0UUL1; -.
DR STRING; 228400.HSM_1490; -.
DR PRIDE; B0UUL1; -.
DR EnsemblBacteria; ACA31241; ACA31241; HSM_1490.
DR KEGG; hsm:HSM_1490; -.
DR HOGENOM; CLU_020581_4_1_6; -.
DR OMA; LGQFQWV; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR005565; Hemolysn_activator_HlyB_C.
DR InterPro; IPR013686; Polypept-transport_assoc_ShlB.
DR InterPro; IPR034746; POTRA.
DR InterPro; IPR035251; ShlB_POTRA.
DR InterPro; IPR027282; TPS.
DR Pfam; PF08479; POTRA_2; 1.
DR Pfam; PF17287; POTRA_3; 1.
DR Pfam; PF03865; ShlB; 1.
DR PIRSF; PIRSF029745; FhaC; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Ion transport; Membrane; Porin; Protein transport;
KW Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..586
FT /note="Outer membrane transporter protein IbpB"
FT /id="PRO_5000311092"
FT DOMAIN 97..172
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
SQ SEQUENCE 586 AA; 66386 MW; 685AE659241C59EC CRC64;
MPKYKYNKIN ILFSCCLLVS FVVAPLVVQA QEDPLVTQAR EAAKEAKPLV QELLHLKNQQ
QFEKVEQNFE KAQRFLEDNR PNQEQIVEQL KSAKDVQTIT KITIDFGGEE IFLDFDEVTK
HYLNQPLSAK TVFALTKELT QVLYNAGYVT SAIGLKSSKI KNGEVEFVVL WGKVNDILVE
EQQASLFKDK AMLFVLPNLK GKVLRIYDVD QLIEILNTGN KTAKVNVIAA NEKSMSNLSI
ERHRTSYPQV SLSLNNSGEG SNAEGRNQAT LSISWSDLLG TNDRWSFSTG YRIYKDRQAN
RQQNYSLSYT QPFSFSTLDI KLSYSGYKKQ LRGIHTHGSS GETKQASFKL SHTLLRNKDM
ILSLYGELEF KRRLSYFGDI RIGKYHNNKL NIGLSYVTNL GHGKLYSDLS YSNGLRWFNA
NHSAYNSHRD KTLRLVSGSI NWQRPFVFFN RGMSYQFRLG AQYGFDSLYG ENQFSIGDEY
TVRGFKGGAG SGDRGFYISQ TVTIPFYPQK SYLSYINPFL GIDIGKVHAK RPHHVVDTFA
GFAFGVKAQI KSLALSLTYA KPINGVGTFE ESNKKSVFYF TGSVSF