ISDH_STAAB
ID ISDH_STAAB Reviewed; 893 AA.
AC Q2YTF7; Q2YTF8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Iron-regulated surface determinant protein H;
DE AltName: Full=Haptoglobin receptor A;
DE AltName: Full=Staphylococcus aureus surface protein I;
DE Flags: Precursor;
GN Name=isdH; Synonyms=harA, sasI; OrderedLocusNames=SAB1591c/SAB1590c;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
CC -!- FUNCTION: Binds human plasma haptoglobin-hemoglobin complexes,
CC haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with
CC significantly higher affinity than haptoglobin alone (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-
CC anchor {ECO:0000305}.
CC -!- DOMAIN: The NEAT 1 domain binds with higher affinity than the NEAT 2
CC domain haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IsdH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI81279.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAI81280.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ938182; CAI81279.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ938182; CAI81280.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q2YTF7; -.
DR BMRB; Q2YTF7; -.
DR SMR; Q2YTF7; -.
DR KEGG; sab:SAB1590c; -.
DR KEGG; sab:SAB1591c; -.
DR HOGENOM; CLU_016167_1_0_9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR CDD; cd06920; NEAT; 1.
DR Gene3D; 2.60.40.1850; -; 3.
DR InterPro; IPR019930; IsdH.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR006635; NEAT_dom.
DR InterPro; IPR037250; NEAT_dom_sf.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF05031; NEAT; 3.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM00725; NEAT; 3.
DR SUPFAM; SSF158911; SSF158911; 3.
DR TIGRFAMs; TIGR03658; IsdH_HarA; 1.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS50978; NEAT; 3.
PE 3: Inferred from homology;
KW Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..862
FT /note="Iron-regulated surface determinant protein H"
FT /id="PRO_0000285181"
FT PROPEP 863..893
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000285182"
FT DOMAIN 105..232
FT /note="NEAT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT DOMAIN 345..471
FT /note="NEAT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT DOMAIN 543..660
FT /note="NEAT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT REGION 42..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 859..863
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 42..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 862
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 893 AA; 100700 MW; 0BFE2B01575D0A60 CRC64;
MNKHHPKLRS FYSIRKSTLG VASVIVSTLF LITSQHQAQA AENTNTSDKI SENQNSNATT
TQPPKDTNQT QPATQPANTA KTYPAADESL KDAIKNPAVE NKEHDIGPRE QVNFLLLDKN
NETQYYHFFS IKDPADVYYT KKKAEVELDI NTASTWKKFE VYENNQKLPV RLVSYSPVPE
DHAYIRFPVS DGTQELKIVS STQIDDGAET NYDYTKLVFA KPIYNDPSLV KSDTNDAVAT
NDQSSSDASN QTNTNTSNQN TSTTNNTSDQ PQATTNMSQP AQPKLSANAD QASSQPAHET
NSNGNTNDKT NESSNQSDVN QQYPPADESL QDAIKNPAII DKEHTADNWR PIDFQMKNDK
GERQFYHYAS TVEPATVIFT KTGPIIELGL KTALTWKKLE VYEGDKKLPV ELVSYDSDKD
YAYIRFPVSN GTREVKIVSS IEYGENIHED YDYTLMVFAQ PITNNPDDYV DEETYNLQKL
LAPYHKAKTL ERQVYELEKL QEKLPEKYKA EYKKKLDQTR VELADQVKSA VTEFENVTPT
NDQLTDVQEA HFVVFESEEN NESVMDGFVE HPFYTATLNG QKYVVMKTKD DSYWKDLIVE
GKRVTTVSKD TKNNSRTLIF PYIPDKAVYN AIVKVVVANI GYEGQYHVRI INQDIKTKDD
DTSQNNTSEH LNGQTVQEDN VTATDTATNN SIETTPREAT DKVDLIEPES DMVKDADSSV
DKDAHHDVDH LSDMSGNTHF DKYDLKEMDT QIAKDTDKGV DNSVGMSSNV DTDKDSNKNK
DKVIQLDHIA DKNKVNNTGT ETNIDTMKYH PISTIKVTDK KTTEHLPSDI HKTVDKTVKT
KEKASTPSKE NKLSQSKMLP KTGETTSSQS WWSLYALLGM LALFIPKFRK ESK
