ID A8AUS0_STRGC Unreviewed; 1575 AA. AC A8AUS0; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 11-DEC-2019, entry version 78. DE SubName: Full=Streptococcal surface protein A {ECO:0000313|EMBL:ABV10916.1}; GN Name=sspA {ECO:0000313|EMBL:ABV10916.1}; GN OrderedLocusNames=SGO_0210 {ECO:0000313|EMBL:ABV10916.1}; OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / OS DL1 / V288). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=467705 {ECO:0000313|Proteomes:UP000001131}; RN [1] {ECO:0000313|EMBL:ABV10916.1, 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). CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000256|PROSITE- CC ProRule:PRU00477, ECO:0000256|SAAS:SAAS01168335}; Peptidoglycan-anchor CC {ECO:0000256|PROSITE-ProRule:PRU00477, ECO:0000256|SAAS:SAAS01168335}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00477}. 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; ABV10916.1; -; Genomic_DNA. DR RefSeq; WP_011999747.1; NC_009785.1. DR STRING; 467705.SGO_0210; -. DR EnsemblBacteria; ABV10916; ABV10916; SGO_0210. DR GeneID; 25052731; -. DR KEGG; sgo:SGO_0210; -. DR eggNOG; ENOG410730G; Bacteria. DR eggNOG; ENOG410Z98C; LUCA. DR HOGENOM; HOG000244333; -. DR OMA; NSWYGAG; -. DR BioCyc; SGOR467705:G1G95-209-MONOMER; -. DR Proteomes; UP000001131; Chromosome. DR GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR Gene3D; 2.60.530.10; -; 1. DR InterPro; IPR026345; Adh_isopep-form_adh_dom. DR InterPro; IPR041324; AgI/II_N. DR InterPro; IPR032300; Antigen_C. DR InterPro; IPR021197; Cross-wall-target_lipo_motif. DR InterPro; IPR013574; Glucan-bd_C/Surface_Ag-I/II_V. DR InterPro; IPR019948; Gram-positive_anchor. DR InterPro; IPR019931; LPXTG_anchor. DR InterPro; IPR036234; SA_I/II_PAC_V_sf. DR InterPro; IPR009578; Surface_Ag_rpt. DR Pfam; PF18652; Adhesin_P1_N; 1. DR Pfam; PF17998; AgI_II_C2; 1. DR Pfam; PF16364; Antigen_C; 1. DR Pfam; PF08363; GbpC; 1. DR Pfam; PF00746; Gram_pos_anchor; 1. DR Pfam; PF06696; Strep_SA_rep; 5. DR SUPFAM; SSF74914; SSF74914; 1. DR TIGRFAMs; TIGR04228; isopep_sspB_C2; 1. DR TIGRFAMs; TIGR03726; strep_RK_lipo; 1. DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1. PE 4: Predicted; KW Cell wall {ECO:0000256|PROSITE-ProRule:PRU00477}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Peptidoglycan-anchor {ECO:0000256|PROSITE-ProRule:PRU00477}; KW Reference proteome {ECO:0000313|Proteomes:UP000001131}; KW Secreted {ECO:0000256|PROSITE-ProRule:PRU00477, KW ECO:0000256|SAAS:SAAS01168298}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..38 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 39..1575 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002717652" FT PROPEP 1543..1575 FT /note="Removed by sortase" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00477" FT /id="PRO_5018350862" FT DOMAIN 1539..1575 FT /note="GRAM_POS_ANCHORING" FT /evidence="ECO:0000259|PROSITE:PS50847" FT REGION 52..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 823..978 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1482..1548 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 142..340 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 352..390 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 395..496 FT /evidence="ECO:0000256|SAM:Coils" FT MOTIF 1539..1543 FT /note="LPXTG sorting signal" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00477" FT COMPBIAS 52..82 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 855..871 FT /note="Pro-rich" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 894..910 FT /note="Pro-rich" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 933..949 FT /note="Pro-rich" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 956..978 FT /note="Pro-rich" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1499..1519 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1542 FT /note="Pentaglycyl murein peptidoglycan amidated threonine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00477" SQ SEQUENCE 1575 AA; 171926 MW; 5F9EA5F22CC2278D CRC64; MNKRKEVFGF RKSKVAKTLC GAVLGAALIA IADQQVLADE VTETNSTANV AVTTTGNPAT NLPEAQGEAT EAASQSQAQA GSKEGALPVE VSADDLNQAV TDAKAAGVNV VQDQTSDKGT ATTAAENAQK QAEIKSDYAK QAEEIKKTTE AYKKEVEAHQ AETDKINAEN KAAEDKYQED LKAHQAEVEK INTANATAKA EYEAKLAQYQ KDLAAVQKAN EDSQLDYQNK LSAYQAELAR VQKANAEAKE AYEKAVKENT AKNAALQAEN EAIKQRNETA KANYDAAMKQ YEADLAAIKK AKEDNDADYQ AKLAAYQAEL ARVQKANADA KAAYEKAVEE NTAKNTAIQA ENEAIKQRNA AAKATYEAAL KQYEADLAAA KKANEDSDAD YQAKLAAYQT ELARVQKANA DAKAAYEKAV EDNKAKNAAL QAENEEIKQR NAAAKTDYEA KLAKYEADLA KYKKELAEYP AKLKAYEDEQ AQIKAALVEL EKNKNQDGYL SKPSAQSLVY DSEPNAQLSL TTNGKMLKAS AVDEAFSHDT AQYSKKILQP DNLNVSYLQQ ADDVTSSMEL YGNFGDKAGW TTTVGNNTEV KFASVLLERG QSVTATYTNL EKSYYNGKKI SKVVFKYTLD SDSKFKNVDK AWLGVFTDPT LGVFASAYTG QEEKDTSIFI KNEFTFYDEN DQPINFDNAL LSVASLNREN NSIEMAKDYS GTFVKISGSS VGEKDGKIYA TETLNFKQGQ GGSRWTMYKN SQPGSGWDSS DAPNSWYGAG AISMSGPTNH VTVGAISATQ VVPSDPVMAV ATGKRPNIWY SLNGKIRAVN VPKITKEKPT PPVAPTEPQA PTYEVEKPLE PAPVAPTYEN EPTPPVKTPD QPEPSKPEEP TYETEKPLEP APVVPTYENE PTPPVKTPDQ PEPSKPEEPT YETEKPLEPA PVAPTYENEP TPPVKTPDQP EPSKPEEPTY DPLPTPPVAP TPKQLPTPPV VPTVHFHYSS LLAQPQINKE IKNEDGVDID RTLVAKQSIV KFELKTEALT AGRPKTTSFV LVDPLPTGYK FDLDATKAAS TGFDTTYDEA SHTVTFKATD ETLATYNADL TKPVETLHPT VVGRVLNDGA TYTNNFTLTV NDAYGIKSNV VRVTTPGKPN DPDNPNNNYI KPTKVNKNKE GLNIDGKEVL AGSTNYYELT WDLDQYKGDK SSKEAIQNGF YYVDDYPEEA LDVRPDLVKV ADEKGNQVSG VSVQQYDSLE AAPKKVQDLL KKANITVKGA FQLFSADNPE EFYKQYVSTG TSLVITDPMT VKSEFGKTGG KYENKAYQID FGNGYATEVV VNNVPKITPK KDVTVSLDPT SENLDGQTVQ LYQTFNYRLI GGLIPQNHSE ELEDYSFVDD YDQAGDQYTG NYKTFSSLNL TMKDGSVIKA GTDLTSQTTA ETDAANGIVT VRFKEDFLQK ISLDSPFQAE TYLQMRRIAI GTFENTYVNT VNKVAYASNT VRTTTPIPRT PDKPTPIPTP KPKDPDKPET PKEPKVPSPK VEDPSAPIPV SVGKELTTLP KTGTNDSSYM PYLGLAALVG VLGLGQLKRK EDESN //