APPA_BACSU
ID APPA_BACSU Reviewed; 543 AA.
AC P42061;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Oligopeptide-binding protein AppA;
DE Flags: Precursor;
GN Name=appA; OrderedLocusNames=BSU11381/BSU11382; ORFNames=BSU11380;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7997159; DOI=10.1111/j.1365-2958.1994.tb00436.x;
RA Koide A., Hoch J.A.;
RT "Identification of a second oligopeptide transport system in Bacillus
RT subtilis and determination of its role in sporulation.";
RL Mol. Microbiol. 13:417-426(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: This protein is a component of an oligopeptide permease, a
CC binding protein-dependent transport system. This APP system can
CC completely substitute for the OPP system in both sporulation and
CC genetic competence. AppA can bind and transport tetra- and
CC pentapeptides but not tripeptides.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AL009126; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U20909; AAA62358.1; -; Genomic_DNA.
DR EMBL; AL009126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; I40545; I40545.
DR PDB; 1XOC; X-ray; 1.55 A; A=25-543.
DR PDBsum; 1XOC; -.
DR AlphaFoldDB; P42061; -.
DR SMR; P42061; -.
DR TCDB; 3.A.1.5.20; the atp-binding cassette (abc) superfamily.
DR PRIDE; P42061; -.
DR InParanoid; P42061; -.
DR EvolutionaryTrace; P42061; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR023765; SBP_5_CS.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Competence; Lipoprotein; Membrane; Palmitate;
KW Peptide transport; Protein transport; Reference proteome; Signal;
KW Sporulation; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 24..543
FT /note="Oligopeptide-binding protein AppA"
FT /id="PRO_0000031791"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="V -> E (in Ref. 1; AAA62358)"
FT /evidence="ECO:0000305"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:1XOC"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 88..99
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1XOC"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1XOC"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:1XOC"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 394..408
FT /evidence="ECO:0007829|PDB:1XOC"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:1XOC"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 436..443
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:1XOC"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 471..480
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 486..503
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 505..511
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:1XOC"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:1XOC"
FT TURN 532..535
FT /evidence="ECO:0007829|PDB:1XOC"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:1XOC"
SQ SEQUENCE 543 AA; 61917 MW; 87E465405D36975B CRC64;
MKRRKTALMM LSVLMVLAIF LSACSGSKSS NSSAKKSAGK PQQGGDLVVG SIGEPTLFNS
LYSTDDASTD IENMLYSFLT KTDEKLNVKL SLAESIKELD GGLAYDVKIK KGVKFHDGKE
LTADDVVFTY SVPLSKDYKG ERGSTYEMLK SVEKKGDYEV LFKLKYKDGN FYNNALDSTA
ILPKHILGNV PIADLEENEF NRKKPIGSGP FKFKEWKQGQ YIKLEANDDY FEGRPYLDTV
TYKVIPDANA AVAQLQAGDI NFFNVPATDY KTAEKFNNLK IVTDLALSYV YIGWNEKNEL
FKDKKVRQAL TTALDRESIV SQVLDGDGEV AYIPESPLSW NYPKDIDVPK FEYNEKKAKQ
MLAEAGWKDT NGDGILDKDG KKFSFTLKTN QGNKVREDIA VVVQEQLKKI GIEVKTQIVE
WSALVEQMNP PNWDFDAMVM GWSLSTFPDQ YDIFHSSQIK KGLNYVWYKN AEADKLMKDA
KSISDRKQYS KEYEQIYQKI AEDQPYTFLY YPNNHMAMPE NLEGYKYHPK RDLYNIEKWW
LAK
