ID   ISDH_STAAW              Reviewed;         895 AA.
AC   Q8NW39;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=MW1674;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB95538.1; -; Genomic_DNA.
DR   RefSeq; WP_001032759.1; NC_003923.1.
DR   PDB; 2LHR; NMR; -; A=467-543.
DR   PDB; 3SZK; X-ray; 3.01 A; C/F=86-229.
DR   PDB; 4FC3; X-ray; 2.26 A; E=321-464.
DR   PDBsum; 2LHR; -.
DR   PDBsum; 3SZK; -.
DR   PDBsum; 4FC3; -.
DR   AlphaFoldDB; Q8NW39; -.
DR   SMR; Q8NW39; -.
DR   EnsemblBacteria; BAB95538; BAB95538; BAB95538.
DR   KEGG; sam:MW1674; -.
DR   HOGENOM; CLU_016167_1_0_9; -.
DR   OMA; TDKGVDN; -.
DR   Proteomes; UP000000418; 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   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..864
FT                   /note="Iron-regulated surface determinant protein H"
FT                   /id="PRO_0000285189"
FT   PROPEP          865..895
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000285190"
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          239..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           861..865
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        657..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..868
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         864
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   HELIX           90..93
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   STRAND          109..112
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   HELIX           125..130
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   STRAND          144..151
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   TURN            153..155
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   STRAND          156..167
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   STRAND          171..175
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   TURN            178..180
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   STRAND          183..189
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   STRAND          195..204
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   STRAND          209..212
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   STRAND          216..221
FT                   /evidence="ECO:0007829|PDB:3SZK"
FT   TURN            326..328
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   HELIX           330..333
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   TURN            337..339
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   STRAND          347..352
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   STRAND          354..357
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   STRAND          361..363
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   HELIX           365..369
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   STRAND          373..380
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   STRAND          383..392
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   TURN            393..395
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   STRAND          396..403
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   STRAND          411..416
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   TURN            417..420
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   STRAND          421..427
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   STRAND          434..443
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   TURN            444..446
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   STRAND          447..460
FT                   /evidence="ECO:0007829|PDB:4FC3"
FT   HELIX           472..486
FT                   /evidence="ECO:0007829|PDB:2LHR"
FT   HELIX           490..503
FT                   /evidence="ECO:0007829|PDB:2LHR"
FT   HELIX           506..529
FT                   /evidence="ECO:0007829|PDB:2LHR"
SQ   SEQUENCE   895 AA;  100847 MW;  797BB0D67F9A0559 CRC64;
     MNKHHPKLRS FYSIRKSILG VASVIVSTLF LITSQHQAQA AENTNTSDKI SENQNNNATT
     TQPPKDTNQT QPATQPANTA KTYPAADESL KDAIKDPALE NKEHDIGPRE QVNFQLLDKN
     NETQYYHFFS IKDPADVYYT KKKAEVELDI NTASTWKKFE VYENNQKLPV RLVSYSPVPE
     DHAYIRFPVS DGTQELKIVS STQIDDGEET NYDYTKLVFA KPIYNDPSLV KSDTNDAVVT
     NDQSSSDASN QTNTNTSNQN TSTINNANNQ PQATTNMSQP AQPKSSANAD QASSQPAHET
     NSNGNTNDKT NESSNQSDVN QQYPPADESL QDAIKNPAII DKEHTADNWR PIDFQMKNDK
     GERQFYHYAS TVEPATVIFT KTGPIIELGL KTASTWKKFE VYEGDKKLPV ELVSYDSDKD
     YAYIRFPVSN GTREVKIVSS IEYGENIHED YDYTLMVFAQ PITNNPDDYV DEETYNLQKL
     LAPYHKAKTL ERQVYELEKL QEKLPEKYKA EYKKKLDQTR VELADQVKSA VTEFENVTPT
     NDQLTDVQEA HFVVFESEEN SESVMDGFVE HPFYTATLNG QKYVVMKTKD DSYWKDLIVE
     GKRVTTVSKD PKNNSRTLIF PYIPDKAVYN AIVKVVVANI GYEGQYHVRI INQDINTKDD
     DTSQNNTSEP LNVQTGQEGK VADTDVAENS STATNPKDAS DKADVIEPDS DVVKDADNNI
     DKDVQHDVDH LSDMSDNNHF DKYDLKEMDT QIAKDTDRNV DKGADNSVGM SSNVDTDKDS
     NKNKDKVIQL NHIADKNNHN GKAAKLDVVK QNYNNTDKVT DKKTTEHLPS DIHKTVDKTV
     KTKEKAGTPS KENKLSQSKM LPKTGETTSS QSWWGLYALL GMLALFIPKF RKESK