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 27-MAR-2024, entry version 105. 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; Bacillota; 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}. 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; 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 KEGG; sam:MW1674; -. DR HOGENOM; CLU_016167_1_0_9; -. 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; 1.20.58.1270; -; 1. DR Gene3D; 2.60.40.1850; -; 3. DR InterPro; IPR048652; Isd_H_B_linker. 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 NCBIfam; TIGR03658; IsdH_HarA; 1. DR NCBIfam; TIGR01167; LPXTG_anchor; 1. DR NCBIfam; TIGR01168; YSIRK_signal; 1. DR PANTHER; PTHR37824; IRON-REGULATED SURFACE DETERMINANT PROTEIN C; 1. DR PANTHER; PTHR37824:SF1; IRON-REGULATED SURFACE DETERMINANT PROTEIN C; 1. DR Pfam; PF20861; Isd_H_B_linker; 1. DR Pfam; PF05031; NEAT; 3. DR SMART; SM00725; NEAT; 3. DR SUPFAM; SSF158911; NEAT domain-like; 3. 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 //