ID A8AXC5_STRGC Unreviewed; 2292 AA.
AC A8AXC5;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Surface-associated protein CshB {ECO:0000313|EMBL:ABV10319.1};
GN Name=cshB {ECO:0000313|EMBL:ABV10319.1};
GN OrderedLocusNames=SGO_1148 {ECO:0000313|EMBL:ABV10319.1};
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV10319.1, ECO:0000313|Proteomes:UP000001131};
RN [1] {ECO:0000313|EMBL:ABV10319.1, ECO:0000313|Proteomes:UP000001131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC {ECO:0000313|Proteomes:UP000001131};
RX PubMed=17720781; DOI=10.1128/JB.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
RN [2] {ECO:0007829|PDB:6YZG}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 211-528.
RX PubMed=36912614; DOI=10.1002/prot.26487;
RA Barringer R., Parnell A.E., Lafita A., Monzon V., Back C.R., Madej M.,
RA Potempa J., Nobbs A.H., Burston S.G., Bateman A., Race P.R.;
RT "Domain shuffling of a highly mutable ligand-binding fold drives adhesin
RT generation across the bacterial kingdom.";
RL Proteins 91:1007-1020(2023).
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; CP000725; ABV10319.1; -; Genomic_DNA.
DR RefSeq; WP_012000554.1; NC_009785.1.
DR PDB; 6YZG; X-ray; 1.40 A; A=211-528.
DR SMR; A8AXC5; -.
DR STRING; 467705.SGO_1148; -.
DR KEGG; sgo:SGO_1148; -.
DR eggNOG; COG2373; Bacteria.
DR HOGENOM; CLU_000552_0_0_9; -.
DR Proteomes; UP000001131; Chromosome.
DR InterPro; IPR026395; CshA_fibril.
DR InterPro; IPR045474; GEVED.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR04225; CshA_fibril_rpt; 15.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR Pfam; PF19076; CshA_repeat; 15.
DR Pfam; PF20009; GEVED; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6YZG};
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000001131};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 12..33
FT /note="YSIRK Gram-positive signal peptide"
FT /evidence="ECO:0000259|Pfam:PF04650"
FT DOMAIN 576..651
FT /note="GEVED"
FT /evidence="ECO:0000259|Pfam:PF20009"
FT DOMAIN 660..764
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 796..902
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 904..1003
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 1005..1104
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 1106..1205
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 1207..1306
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 1308..1406
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 1409..1507
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 1510..1608
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 1611..1710
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 1712..1811
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 1813..1911
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 1914..2013
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 2018..2108
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 2115..2203
FT /note="CshA"
FT /evidence="ECO:0000259|Pfam:PF19076"
FT DOMAIN 2248..2289
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|Pfam:PF00746"
FT REGION 57..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1814..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2004..2029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2232..2264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1715..1737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1814..1834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2005..2029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2240..2254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2292 AA; 243820 MW; 2E419B9FC712C0C5 CRC64;
MGKDLFNTHL SKFSIRKLNI GVCSVLLSTL ILLGTALQVS AEETSTSGFQ NEISKADVTE
SPVISDESTT YQQVQNTEKT ESVPDSEKSQ SADNPIQRNS GLEGVEKTTD SIQAKSTDDI
KSTVVQQGST ESQVVDENSG VKTDVTQASR SRRVRRDATP TGQQNGVTTG VPIGTGPAGA
DDATSKPRVP KPSLDESLKK DSVQLAKQIS WLDFSDSASW KNLDQRGGLK VGTTFTKEIS
PGYVVTLTVK ELKPFNSTEI YKKRVAGTAT EGTYNPDAEN GFLTSAPYYG KTPPPSVTGA
AQNEWTTIRD QGFNTQKRKT QLVYPMNSTN WGVKFDIEAT YLGKRVAPTV VMADGEDANP
GEFAIFTTNG TGWEYMGEWK MKSPAKEAYT VITKKMLDDE DVKRRGLLIL KDKSVDWYKY
LSPDTVTGGL GSQVFGPNRS NERTVPVVMT RGASEVGFYV ASSGQQAMMM GFLVVDVSDA
PESYGEAFHT ISTRDSVTND PINQPYLGTT PADIDVESSN DWVLDDKKEH KDEGASQLLA
DDQLSTSNDL LDLDKAKNGT YTIKIKANPN GNAKSYVKAW IDFNNDGVFN ESEGSNLQEI
TAAGDYTLTF NANPNISGGQ VDKLGMRFRI ATNKGDIEQP TGIAFSGEVE DMLLHRIYPP
KGEKQTTDGF TGETQTAVLH FTPKGTDRSD DSVNAVMSTQ APQILDKQGQ VLTAVDGNYI
RPEGTYQVTV NGNDVQVTFT PKADFSGTAD GINIRWTDQN GTSTGWASTD ASDPNMNDLL
NTMDGSYMPT VRKIPNYESS GLQGLEQNKT LVFNDDDANT PPVTPDTTRP ASFVDASGQP
VAGNTVPAMS NGQQVGTYEL DPNTGQVTFK PIKTFYGTPD LVVVQVSDTD GKAHRARYQP
KVTQVTPRST NAESTGLQGQ AQNGKPTFTA GDQQIPIDMS KAMTFDNGTN TLEVANEGTY
TINSDDTITF KPLKQFTGKA TPVTVKRVDE NGTEVTATYT PNVTKVTPTS TPATSSGPQG
VPQTGTPVFK EGDPAVPIDY NKQMTFDNDQ PKKIVAGVGE YTINSDGSIT FTPDKQYVGT
PAPVTVKRVD ENGTEVRATY TPTVTKVTPA GTGDKTEGLQ GQVQEGHVTF TPGHASVPFP
AETTPLFDNG LTVKEVLNVG KFEVDANGKV TFTPDKQFKG ETPELELTRM DANGTPVTVK
YQAVVKEVTP TSTDATSNGI QGQPQKGTPT FTEGNPLVPI DDTKPMTFED GQSTKTVPGV
GEYSINPDGS ITFTPDKQYV GTPTPVTVKR VDKNGTEVTA TYTPSVTKVT PTGTGATSTG
PQGLPQTGAP TFQGGDPLVP IDETVEPTFE DGSKEKSIPG QGTYTIAPDG TVTFTPDKQF
VGKPDPVMVK RVDKNGTPVT ATYSPEFTKV TPTGTGATST GPQDLPQTGT PTFQGGDPLV
PIDETVEPTF EDGSKEKSIP GQGTYTIAPD GTVTFTPDKQ FVGKPDPVMV KRVDKNGTPV
TATYSPEFTK VTPTGTGATS TGPQGLPQTG TPTFQGGDPL VPIDETVEPT FEDGSKEKSI
PGQGTYTIAS DGTVTFTPDK QFVGKPDPVT VKRVDKNGTP VTATYSPEFT KVTPTGTGDK
TEGLQGQVQE GKVTFTPGHD LVPFPADSTP LFDNGTAVKE VPNVGKFEVD ADGKVTFTPD
KQFKGETPEL ELTRVDANGT PVTVKYQAVV KEVTPTSTDA TSNGVQGQPQ KGTPTFTEGN
PLVPIDDTKP MTFGDGQSTK TVPGVGEYSI NPDGSITFTP EKQYVGTPTP VTVKRVDKNG
TEVTATYTPT VTKVTPTSTN ATSTGPQGLP QTGTPTFEGG DPLVPIDETV EPTFEDGSKE
KVILGQGTYT IAPDGTVTFT PDKQFVGKPD PVTVKRVDKN GTPVTATYSP EFTKVTPIGK
DASSENIKGL VQTGTPTFEG GDPLVPIDET VAPTFEDGST EKVIPGEGIY TISPDGTVTF
TPEADFVGKG TGVTIVRKDK NGTPVTASYR PTVVDPSTGQ DTTSTGAKGQ TQVATPAFEG
HIDSTVPPTF EDGSTTLVVP GEGSYTIDKD GHITFTPEAD FVGTAKGVVV KRLDIYGNVV
TAQYTPTVIG QTRVEDVTSD GLKGQTQTGK PIFEGDVDLT VAPTFEDGST EKVVPGEGTY
TISPDGVVTF VPEPNFVGTA KGVVVIRKDR NGQTISASYT PRVTEIPVVP NRPSTPEQPK
VPVIPAEPAV AVQTPKAEER VEPVYVDPKD EKGVLPRTGS QTSDQTASGL LAAIASLTFF
GLANRKKKSE ED
//
