ID   HBPA_HAEIN              Reviewed;         547 AA.
AC   P33950;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Heme-binding protein A;
DE   AltName: Full=Hemin-binding lipoprotein;
DE   Flags: Precursor;
GN   Name=hbpA; Synonyms=dppA; OrderedLocusNames=HI_0853;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=DL42 / Serotype B;
RX   PubMed=1339409; DOI=10.1128/iai.60.6.2257-2266.1992;
RA   Hanson M.S., Slaughter C., Hansen E.J.;
RT   "The hbpA gene of Haemophilus influenzae type b encodes a heme-binding
RT   lipoprotein conserved among heme-dependent Haemophilus species.";
RL   Infect. Immun. 60:2257-2266(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [3]
RP   POSSIBLE FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=DL42 / Serotype B;
RX   PubMed=2041470; DOI=10.1111/j.1365-2958.1991.tb02107.x;
RA   Hanson M.S., Hansen E.J.;
RT   "Molecular cloning, partial purification, and characterization of a haemin-
RT   binding lipoprotein from Haemophilus influenzae type b.";
RL   Mol. Microbiol. 5:267-278(1991).
CC   -!- FUNCTION: Important role in heme acquisition or metabolism.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2041470};
CC       Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303,
CC       ECO:0000269|PubMed:2041470}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC22512.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M88134; AAA73214.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M84028; AAA24962.1; -; Genomic_DNA.
DR   EMBL; L42023; AAC22512.1; ALT_INIT; Genomic_DNA.
DR   PIR; D64098; D64098.
DR   PIR; T45066; T45066.
DR   RefSeq; NP_439013.1; NC_000907.1.
DR   RefSeq; WP_005670186.1; NC_000907.1.
DR   AlphaFoldDB; P33950; -.
DR   SMR; P33950; -.
DR   STRING; 71421.HI_0853; -.
DR   TCDB; 3.A.1.5.27; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; AAC22512; AAC22512; HI_0853.
DR   KEGG; hin:HI_0853; -.
DR   PATRIC; fig|71421.8.peg.894; -.
DR   eggNOG; COG0747; Bacteria.
DR   HOGENOM; CLU_017028_7_0_6; -.
DR   PhylomeDB; P33950; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0042938; P:dipeptide transport; IBA:GO_Central.
DR   GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR   InterPro; IPR030678; Peptide/Ni-bd.
DR   InterPro; IPR039424; SBP_5.
DR   InterPro; IPR023765; SBP_5_CS.
DR   InterPro; IPR000914; SBP_5_dom.
DR   PANTHER; PTHR30290; PTHR30290; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
DR   PIRSF; PIRSF002741; MppA; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Direct protein sequencing; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000305"
FT   CHAIN           19..547
FT                   /note="Heme-binding protein A"
FT                   /id="PRO_0000031790"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
FT   VARIANT         48..49
FT                   /note="KA -> NS (in strain: DL42)"
FT   VARIANT         181
FT                   /note="T -> N (in strain: DL42)"
FT   VARIANT         240
FT                   /note="H -> N (in strain: DL42)"
FT   VARIANT         343
FT                   /note="T -> I (in strain: DL42)"
FT   VARIANT         375
FT                   /note="A -> V (in strain: DL42)"
SQ   SEQUENCE   547 AA;  60661 MW;  7755E2164A40CB31 CRC64;
     MKLKATLTLA AATLVLAACD QSSSANKSTA QTEAKSSSNN TFVYCTAKAP LGFSPALIIE
     GTSYNASSQQ VYNRLVEFKK GSTDIEPALA ESWEISDDGL SYTFHLRKGV KFHTTKEFTP
     TRDFNADDVV FSFQRQLDPN HPYHNVSKGT YPYFKAMKFP ELLKSVEKVD DNTIRITLNK
     TDATFLASLG MDFISIYSAE YADSMLKAGK PETLDSRPVG TGPFVFVDYK TDQAIQYVAH
     ENYWKGRTPL DRLVISIVPD ATTRYAKLQA GTCDLILFPN VADLAKMKTD PKVQLLEQKG
     LNVAYIAFNT EKAPFDNVKV RQALNYAVDK KAIIEAVYQG AGTSAKNPLP PTIWSYNDEI
     QDYPYDPEKA KQLLAEAGYP NGFETDFWIQ PVIRASNPNP KRMAELIMAD WAKIGVKTNP
     VTYEWADYRK RAKEGELTAG IFGWSGDNGD PDNFLSPLLG SSNIGNSNMA RFNNSEFDAL
     LNEAIGLTNK EERAKLYKQA QVIVHNQAPW IPVAHSVGFA PLSPRVKGYV QSPFGYDAFY
     GVSVDGK