ID A8AUS0_STRGC Unreviewed; 1575 AA. AC A8AUS0; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 08-MAY-2019, entry version 75. 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 RT response 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- CC anchor {ECO:0000256|PROSITE-ProRule:PRU00477, CC ECO:0000256|SAAS:SAAS01168335}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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:InterPro. 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 Complete proteome {ECO:0000313|Proteomes:UP000001131}; 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 {ECO:0000256|SAM:SignalP}. FT CHAIN 39 1575 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002717652. FT PROPEP 1543 1575 Removed by sortase. {ECO:0000256|PROSITE- FT ProRule:PRU00477}. FT /FTId=PRO_5018350862. FT DOMAIN 1539 1575 GRAM_POS_ANCHORING. {ECO:0000259|PROSITE: FT PS50847}. FT COILED 142 340 {ECO:0000256|SAM:Coils}. FT COILED 352 390 {ECO:0000256|SAM:Coils}. FT COILED 395 496 {ECO:0000256|SAM:Coils}. FT MOTIF 1539 1543 LPXTG sorting signal. FT {ECO:0000256|PROSITE-ProRule:PRU00477}. FT MOD_RES 1542 1542 Pentaglycyl murein peptidoglycan amidated FT threonine. {ECO:0000256|PROSITE-ProRule: FT 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 //