ISDH_STAA3
ID ISDH_STAA3 Reviewed; 895 AA.
AC Q2FG07;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=SAUSA300_1677;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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; CP000255; ABD20516.1; -; Genomic_DNA.
DR RefSeq; WP_001032773.1; NZ_CP027476.1.
DR PDB; 4IJ2; X-ray; 4.24 A; E/F/G/H=326-660.
DR PDB; 4XS0; X-ray; 2.55 A; C=326-660.
DR PDBsum; 4IJ2; -.
DR PDBsum; 4XS0; -.
DR AlphaFoldDB; Q2FG07; -.
DR BMRB; Q2FG07; -.
DR SMR; Q2FG07; -.
DR EnsemblBacteria; ABD20516; ABD20516; SAUSA300_1677.
DR KEGG; saa:SAUSA300_1677; -.
DR HOGENOM; CLU_016167_1_0_9; -.
DR OMA; TDKGVDN; -.
DR Proteomes; UP000001939; 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..864
FT /note="Iron-regulated surface determinant protein H"
FT /id="PRO_0000285195"
FT PROPEP 865..895
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000285196"
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 HELIX 330..333
FT /evidence="ECO:0007829|PDB:4XS0"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:4XS0"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:4XS0"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:4XS0"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 434..443
FT /evidence="ECO:0007829|PDB:4XS0"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 447..460
FT /evidence="ECO:0007829|PDB:4XS0"
FT HELIX 475..486
FT /evidence="ECO:0007829|PDB:4XS0"
FT HELIX 490..503
FT /evidence="ECO:0007829|PDB:4XS0"
FT HELIX 506..533
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 552..556
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:4XS0"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 571..578
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 581..590
FT /evidence="ECO:0007829|PDB:4XS0"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 605..610
FT /evidence="ECO:0007829|PDB:4XS0"
FT HELIX 611..613
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 615..621
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 628..636
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:4XS0"
FT STRAND 643..652
FT /evidence="ECO:0007829|PDB:4XS0"
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
