ID   ISDH_STAAC              Reviewed;         895 AA.
AC   Q5HF43;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=SACOL1781;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
RN   [2]
RP   FUNCTION, AND ROLE OF THE NEAT DOMAINS.
RX   PubMed=12823809; DOI=10.1046/j.1365-2958.2003.03542.x;
RA   Dryla A., Gelbmann D., von Gabain A., Nagy E.;
RT   "Identification of a novel iron regulated staphylococcal surface protein
RT   with haptoglobin-haemoglobin binding activity.";
RL   Mol. Microbiol. 49:37-53(2003).
RN   [3]
RP   STRUCTURE BY NMR OF 86-221, AND BINDING PROPERTIES OF THE NEAT DOMAINS.
RX   PubMed=17041047; DOI=10.1128/jb.01366-06;
RA   Dryla A., Hoffmann B., Gelbmann D., Giefing C., Hanner M., Meinke A.,
RA   Anderson A.S., Koppensteiner W., Konrat R., von Gabain A., Nagy E.;
RT   "High-affinity binding of the staphylococcal harA protein to haptoglobin
RT   and hemoglobin involves a domain with an antiparallel eight-stranded beta-
RT   barrel fold.";
RL   J. Bacteriol. 189:254-264(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.
CC       {ECO:0000269|PubMed:12823809}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-
CC       anchor {ECO:0000305}.
CC   -!- DOMAIN: The NEAT 1 domain is formed by an antiparallel eight-stranded
CC       beta-barrel fold. It binds with higher affinity than the NEAT 2 domain
CC       haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin.
CC   -!- SIMILARITY: Belongs to the IsdH family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW38309.1; -; Genomic_DNA.
DR   RefSeq; WP_001032773.1; NC_002951.2.
DR   AlphaFoldDB; Q5HF43; -.
DR   BMRB; Q5HF43; -.
DR   SMR; Q5HF43; -.
DR   EnsemblBacteria; AAW38309; AAW38309; SACOL1781.
DR   KEGG; sac:SACOL1781; -.
DR   HOGENOM; CLU_016167_1_0_9; -.
DR   OMA; TDKGVDN; -.
DR   Proteomes; UP000000530; 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   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_0000285183"
FT   PROPEP          865..895
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000285184"
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..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..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        700..720
FT                   /note="Basic and acidic 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"
SQ   SEQUENCE   895 AA;  100935 MW;  A21F8D02EC49729C CRC64;
     MNKHHPKLRS FYSIRKSTLG VASVIVSTLF LITSQHQAQA AENTNTSDKI SENQNNNATT
     TQPPKDTNQT QPATQPANTA KNYPAADESL KDAIKDPALE NKEHDIGPRE QVNFQLLDKN
     NETQYYHFFS IKDPADVYYT KKKAEVELDI NTASTWKKFE VYENNQKLPV RLVSYSPVPE
     DHAYIRFPVS DGTQELKIVS STQIDDGEET NYDYTKLVFA KPIYNDPSLV KSDTNDAVVT
     NDQSSSVASN QTNTNTSNQN TSTINNANNQ PQATTNMSQP AQPKSSTNAD 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
     NDQLTDLQEA HFVVFESEEN SESVMDGFVE HPFYTATLNG QKYVVMKTKD DSYWKDLIVE
     GKRVTTVSKD PKNNSRTLIF PYIPDKAVYN AIVKVVVANI GYEGQYHVRI INQDINTKDD
     DTSQNNTSEP LNVQTGQEGK VADTDVAENS STATNPKDAS DKADVIEPES DVVKDADNNI
     DKDVQHDVDH LSDMSDNNHF DKYDLKEMDT QIAKDTDRNV DKDADNSVGM SSNVDTDKDS
     NKNKDKVIQL NHIADKNNHT GKAAKLDVVK QNYNNTDKVT DKKTTEHLPS DIHKTVDKTV
     KTKEKAGTPS KENKLSQSKM LPKTGETTSS QSWWGLYALL GMLALFIPKF RKESK