ID   ISDH_STAAN              Reviewed;         891 AA.
AC   Q99TD3;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=SA1552;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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}.
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DR   EMBL; BA000018; BAB42820.1; -; Genomic_DNA.
DR   PIR; G89957; G89957.
DR   RefSeq; WP_001032807.1; NC_002745.2.
DR   PDB; 4WJG; X-ray; 3.10 A; 3/D/I/N/S/X=86-229.
DR   PDBsum; 4WJG; -.
DR   AlphaFoldDB; Q99TD3; -.
DR   SMR; Q99TD3; -.
DR   EnsemblBacteria; BAB42820; BAB42820; BAB42820.
DR   KEGG; sau:SA1552; -.
DR   HOGENOM; CLU_016167_1_0_9; -.
DR   OMA; TDKGVDN; -.
DR   Proteomes; UP000000751; Chromosome.
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   1: Evidence at protein level;
KW   3D-structure; Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..860
FT                   /note="Iron-regulated surface determinant protein H"
FT                   /id="PRO_0000285191"
FT   PROPEP          861..891
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000285192"
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..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          835..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           857..861
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        657..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..772
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         860
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   HELIX           90..93
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   STRAND          109..112
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   HELIX           125..130
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   STRAND          141..151
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   STRAND          156..163
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   STRAND          171..176
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   TURN            177..180
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   STRAND          182..189
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   STRAND          195..203
FT                   /evidence="ECO:0007829|PDB:4WJG"
FT   STRAND          209..221
FT                   /evidence="ECO:0007829|PDB:4WJG"
SQ   SEQUENCE   891 AA;  100467 MW;  BE8FE3268B7DDC61 CRC64;
     MNKHHPKLRS FYSIRKSTLG VASVIVSTLF LITSQHQAQA AENTNTSDKI SENQNNNATT
     TQQPKDTNQT QPATQPVITA KNYPAADESL KDAIKDPALE NKEHDIGPRE QVNFQLLDKN
     NETQYYHFFS IKDPADVYYT KKKAEVELDI NTASTWKKFE VYENNQKLPV RLVSYSPVPE
     DHAYIRFPVS DGTQELKIVS STQIDDGEET NYDYTKLVFA KPIYNDPSLV KSDTNDAVVT
     NDQSSSDASN QTNTNTSNQN TSTTNNANNQ PQATTNMSQP AQPKSSANAD QASSQPAHET
     NSNGNTNDKT NESSNQSDVN QQYPPADESL QDAIKNPAII DKEHTADNWR PIDFQMKNDK
     GERQFYHYAS TVEPATVIFT KTGPVIELGL KTASTWKKFE VYEGDKKLPV ELVSYDSDKD
     YAYIRFPVSN GTRDVKNVSS IEYGENIHED YDYTLMVFAQ PITNNPDDYV DEETYNLQKL
     LAPYHKAKTL ERQVYELEKL QEKLPEKYKA EYKKKLDQTR VELADQVKSA VTEFENVTPT
     NDQLTDLQEA HFVVFESEEN SESVMDGFVE HPFYTATLNG QKYVVMKTKD DSYWKDLIVE
     GKRVTTVSKD PKNNSRTLIF PYIPDKAVYN AIVKVVVANI GYEGQYHVRI INQDINTKDD
     DTSQNNTSEP LNVQTGQEGK VADTDVAENS STATNPKDAS DKADVIEPES DVVKDADNNI
     DKDVQHDVDH LSDMSDNNHF DKYDLKEMDT QIAKDTDRNV DNSVGMSSNV DTDKDSNKNK
     DKVIQLAHIA DKNNHTGKAA KLDVVKQNYN NTDKVTDKKT TEHLPSDIHK TVDKTVKTKE
     KAGTPSKENK LSQSKMLPKT GETTSSQSWW GLYALLGMLA LFIPKFRKES K