ISDH_STAA8
ID ISDH_STAA8 Reviewed; 895 AA.
AC Q2FXJ2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=SAOUHSC_01843;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, AND REGULATION BY FUR AND IRON.
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).
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 -!- INDUCTION: Expression was observed only in the late logarithmic and
CC stationary phase. Repressed by the ferric uptake repressor (fur)
CC protein in the presence of iron.
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; CP000253; ABD30910.1; -; Genomic_DNA.
DR RefSeq; WP_001032766.1; NZ_LS483365.1.
DR RefSeq; YP_500348.1; NC_007795.1.
DR PDB; 6TB2; X-ray; 2.90 A; D/E=321-655.
DR PDBsum; 6TB2; -.
DR AlphaFoldDB; Q2FXJ2; -.
DR BMRB; Q2FXJ2; -.
DR SMR; Q2FXJ2; -.
DR STRING; 1280.SAXN108_1760; -.
DR ABCD; Q2FXJ2; 2 sequenced antibodies.
DR EnsemblBacteria; ABD30910; ABD30910; SAOUHSC_01843.
DR GeneID; 3920522; -.
DR KEGG; sao:SAOUHSC_01843; -.
DR PATRIC; fig|93061.5.peg.1679; -.
DR eggNOG; COG5386; Bacteria.
DR HOGENOM; CLU_016167_1_0_9; -.
DR OMA; TDKGVDN; -.
DR PRO; PR:Q2FXJ2; -.
DR Proteomes; UP000008816; 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; Reference proteome; Repeat;
KW 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_0000285193"
FT PROPEP 865..895
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000285194"
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"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:6TB2"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:6TB2"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6TB2"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 371..379
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:6TB2"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:6TB2"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 432..443
FT /evidence="ECO:0007829|PDB:6TB2"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 447..462
FT /evidence="ECO:0007829|PDB:6TB2"
FT HELIX 472..480
FT /evidence="ECO:0007829|PDB:6TB2"
FT HELIX 482..486
FT /evidence="ECO:0007829|PDB:6TB2"
FT HELIX 490..502
FT /evidence="ECO:0007829|PDB:6TB2"
FT TURN 506..508
FT /evidence="ECO:0007829|PDB:6TB2"
FT HELIX 509..524
FT /evidence="ECO:0007829|PDB:6TB2"
FT HELIX 526..532
FT /evidence="ECO:0007829|PDB:6TB2"
FT TURN 533..536
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 552..562
FT /evidence="ECO:0007829|PDB:6TB2"
FT HELIX 564..568
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 571..578
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 581..590
FT /evidence="ECO:0007829|PDB:6TB2"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 605..610
FT /evidence="ECO:0007829|PDB:6TB2"
FT TURN 611..614
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 615..621
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 628..637
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 640..642
FT /evidence="ECO:0007829|PDB:6TB2"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:6TB2"
SQ SEQUENCE 895 AA; 100947 MW; A5F94CEFD7428F9C 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 ISTINNANNQ 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
