ASP1_STRGN
ID ASP1_STRGN Reviewed; 526 AA.
AC Q9AET9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Accessory Sec system protein Asp1;
DE AltName: Full=Accessory secretory protein Asp1;
DE AltName: Full=Orf1;
GN Name=asp1;
OS Streptococcus gordonii.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1302;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M99;
RX PubMed=12010500; DOI=10.1046/j.1365-2958.2002.02949.x;
RA Bensing B.A., Sullam P.M.;
RT "An accessory sec locus of Streptococcus gordonii is required for export of
RT the surface protein GspB and for normal levels of binding to human
RT platelets.";
RL Mol. Microbiol. 44:1081-1094(2002).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=M99;
RX PubMed=15049820; DOI=10.1111/j.1365-2958.2004.03978.x;
RA Takamatsu D., Bensing B.A., Sullam P.M.;
RT "Genes in the accessory sec locus of Streptococcus gordonii have three
RT functionally distinct effects on the expression of the platelet-binding
RT protein GspB.";
RL Mol. Microbiol. 52:189-203(2004).
CC -!- FUNCTION: Part of the accessory SecA2/SecY2 system specifically
CC required to export GspB, a serine-rich repeat cell wall protein encoded
CC upstream in the same operon. {ECO:0000269|PubMed:15049820}.
CC -!- SUBUNIT: Part of the accessory SecA2/SecY2 protein translocation
CC apparatus required to export cell wall protein GspB.
CC -!- DISRUPTION PHENOTYPE: Loss of export of cell wall protein GspB, the
CC protein accumulates intracellularly in protoplasts.
CC {ECO:0000269|PubMed:15049820}.
CC -!- SIMILARITY: Belongs to the accessory Sec system protein Asp1 family.
CC {ECO:0000305}.
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DR EMBL; AY028381; AAK16998.1; -; Genomic_DNA.
DR RefSeq; WP_061598990.1; NZ_RJVY01000036.1.
DR PDB; 5VAE; X-ray; 3.11 A; A/C/E/G=1-526.
DR PDB; 5VAF; X-ray; 2.77 A; A/B/C/D=1-526.
DR PDBsum; 5VAE; -.
DR PDBsum; 5VAF; -.
DR AlphaFoldDB; Q9AET9; -.
DR SMR; Q9AET9; -.
DR TCDB; 3.A.5.10.1; the general secretory pathway (sec) family.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR022372; Accessory_SS_Asp1.
DR Pfam; PF16993; Asp1; 1.
DR TIGRFAMs; TIGR03713; acc_sec_asp1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Protein transport; Translocation; Transport.
FT CHAIN 1..526
FT /note="Accessory Sec system protein Asp1"
FT /id="PRO_0000414196"
FT COILED 359..386
FT /evidence="ECO:0000255"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5VAE"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 132..150
FT /evidence="ECO:0007829|PDB:5VAF"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 154..172
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5VAF"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5VAE"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:5VAE"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 353..361
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 364..381
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:5VAE"
FT STRAND 409..416
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 419..428
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 441..450
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:5VAF"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 478..486
FT /evidence="ECO:0007829|PDB:5VAF"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 490..504
FT /evidence="ECO:0007829|PDB:5VAF"
FT HELIX 508..525
FT /evidence="ECO:0007829|PDB:5VAF"
SQ SEQUENCE 526 AA; 62423 MW; AF5C66AE4C5A4213 CRC64;
MYYFIPSWSG SGKRVWHRDI IPWYRSMQRL EFDDTIHQIR IFHSENLPVK LLLQAYMPHA
RYFLHRQDIF ETEYYSVFDE IQAVESNDMQ VLQIKDLEWE DDCEFIYTPF LIIVRRQGQL
YAHVEFGVEG FISFIKFFKD DQLEKLNIFD DRGFVSSIVY YEDGQEVCQD YLNPNGDWRI
REYLKFENSH VVVNPVFSRD FDKLEYECMP DLILEKLGYY ISHNVEEDSR FVVAAQPFTN
QGVLDLLPQH SHSILSFFHE RNQASNIENL KADLEYADLV LTDRMDFKET LQNYFPLQAE
KIHYLSPFDT RLQLGKSQQR HESKIFYQID LSELLNDYAI FKVLFYVAQH PDTELVIGVY
NAWQEGIKQV ENKVEELISD YLDLKDFIKK SFKNNQAENP LPENQELEYR FRIRNITDEL
SLIQELDDTR LIIDLSQQPN LYTQIAGISA GIPQINLVAS DYVTHLQNGY ILDSISQLAV
AADYYLQGLK NWNQALIYSI EKIKLNTGHQ VIKRWEKWLK EAIDEK
