SCIN_STAAM
ID SCIN_STAAM Reviewed; 116 AA.
AC Q931M7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Staphylococcal complement inhibitor;
DE Short=SCIN;
DE Flags: Precursor;
GN Name=scn; OrderedLocusNames=SAV1942;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
CC -!- FUNCTION: Involved in countering the first line of host defense
CC mechanisms. Efficiently inhibits opsonization, phagocytosis and killing
CC of S.aureus by human neutrophils. Acts by binding and stabilizing human
CC C3 convertases (C4b2a and C3bBb), leading to their inactivation. The
CC convertases are no longer able to cleave complement C3, therefore
CC preventing further C3b deposition on the bacterial surface and
CC phagocytosis of the bacterium. Also prevents C5a-induced neutrophil
CC responses (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SCIN family. {ECO:0000305}.
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DR EMBL; BA000017; BAB58104.1; -; Genomic_DNA.
DR RefSeq; WP_000702263.1; NC_002758.2.
DR PDB; 3L3O; X-ray; 3.40 A; M/P=32-116.
DR PDB; 3L5N; X-ray; 7.54 A; M=32-116.
DR PDB; 3NMS; X-ray; 4.10 A; M=32-116.
DR PDB; 3OHX; X-ray; 3.50 A; M/P=32-116.
DR PDB; 6RUV; X-ray; 6.15 A; N/Q=31-116.
DR PDBsum; 3L3O; -.
DR PDBsum; 3L5N; -.
DR PDBsum; 3NMS; -.
DR PDBsum; 3OHX; -.
DR PDBsum; 6RUV; -.
DR AlphaFoldDB; Q931M7; -.
DR SMR; Q931M7; -.
DR PaxDb; Q931M7; -.
DR EnsemblBacteria; BAB58104; BAB58104; SAV1942.
DR KEGG; sav:SAV1942; -.
DR HOGENOM; CLU_166895_0_0_9; -.
DR OMA; LARTMYP; -.
DR PhylomeDB; Q931M7; -.
DR BioCyc; SAUR158878:SAV_RS10640-MON; -.
DR EvolutionaryTrace; Q931M7; -.
DR PRO; PR:Q931M7; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 1.20.1270.10; -; 1.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR021612; SCIN.
DR Pfam; PF11546; CompInhib_SCIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Secreted; Signal; Virulence.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..116
FT /note="Staphylococcal complement inhibitor"
FT /id="PRO_0000319871"
FT REGION 62..79
FT /note="Essential for activity"
FT /evidence="ECO:0000250"
FT HELIX 38..55
FT /evidence="ECO:0007829|PDB:3L3O"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:3L3O"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:3L3O"
FT HELIX 69..88
FT /evidence="ECO:0007829|PDB:3L3O"
FT HELIX 91..113
FT /evidence="ECO:0007829|PDB:3L3O"
SQ SEQUENCE 116 AA; 13067 MW; 6C30E481973D19E9 CRC64;
MKIRKSILAG TLAIVLASPL VTNLDKNEAQ ASTSLPTSNE YQNEKLANEL KSLLDELNVN
ELATGSLNTY YKRTIKISGQ KAMYALKSKD FKKMSEAKYQ LQKIYNEIDE ALKSKY
