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GERQ_BACSU
ID   GERQ_BACSU              Reviewed;         181 AA.
AC   P39620;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Spore coat protein GerQ;
GN   Name=gerQ; Synonyms=ywdL; OrderedLocusNames=BSU37920; ORFNames=ipa-62r;
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=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
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).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=12644503; DOI=10.1128/jb.185.7.2315-2329.2003;
RA   Ragkousi K., Eichenberger P., van Ooij C., Setlow P.;
RT   "Identification of a new gene essential for germination of Bacillus
RT   subtilis spores with Ca2+-dipicolinate.";
RL   J. Bacteriol. 185:2315-2329(2003).
RN   [4]
RP   SUBUNIT.
RC   STRAIN=168;
RX   PubMed=15317760; DOI=10.1128/jb.186.17.5567-5575.2004;
RA   Ragkousi K., Setlow P.;
RT   "Transglutaminase-mediated cross-linking of GerQ in the coats of Bacillus
RT   subtilis spores.";
RL   J. Bacteriol. 186:5567-5575(2004).
RN   [5]
RP   SUBUNIT.
RC   STRAIN=168 / MB24;
RX   PubMed=16267299; DOI=10.1128/jb.187.22.7753-7764.2005;
RA   Zilhao R., Isticato R., Martins L.O., Steil L., Voelker U., Ricca E.,
RA   Moran C.P. Jr., Henriques A.O.;
RT   "Assembly and function of a spore coat-associated transglutaminase of
RT   Bacillus subtilis.";
RL   J. Bacteriol. 187:7753-7764(2005).
RN   [6]
RP   PTM, SUBCELLULAR LOCATION, CROSS-LINKING DONOR SITES, AND MUTAGENESIS OF
RP   1-MET--LYS-5; LYS-2; LYS-4 AND LYS-5.
RC   STRAIN=168;
RX   PubMed=16936016; DOI=10.1128/jb.01116-06;
RA   Monroe A., Setlow P.;
RT   "Localization of the transglutaminase cross-linking sites in the Bacillus
RT   subtilis spore coat protein GerQ.";
RL   J. Bacteriol. 188:7609-7616(2006).
RN   [7]
RP   SUBUNIT.
RC   STRAIN=168;
RX   PubMed=16751597; DOI=10.1093/jb/mvj096;
RA   Kuwana R., Okuda N., Takamatsu H., Watabe K.;
RT   "Modification of GerQ reveals a functional relationship between Tgl and
RT   YabG in the coat of Bacillus subtilis spores.";
RL   J. Biochem. 139:887-901(2006).
RN   [8]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=19933362; DOI=10.1128/jb.01103-09;
RA   Imamura D., Kuwana R., Takamatsu H., Watabe K.;
RT   "Localization of proteins to different layers and regions of Bacillus
RT   subtilis spore coats.";
RL   J. Bacteriol. 192:518-524(2010).
CC   -!- FUNCTION: Essential for the localization of CwlJ in the spore coat and
CC       for spore germination triggered by calcium and dipicolinic acid (DPA).
CC       Its assembly into the spore coat is dependent on the coat morphogenetic
CC       proteins CotE and SpoIVA. {ECO:0000269|PubMed:12644503}.
CC   -!- SUBUNIT: Multimer. Is cross-linked by Tgl and YabG into an insoluble
CC       high-molecular-mass complex that appears very late in sporulation.
CC       {ECO:0000269|PubMed:15317760, ECO:0000269|PubMed:16267299,
CC       ECO:0000269|PubMed:16751597}.
CC   -!- SUBCELLULAR LOCATION: Spore coat {ECO:0000269|PubMed:12644503,
CC       ECO:0000269|PubMed:16936016, ECO:0000269|PubMed:19933362}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during sporulation in mother cell
CC       compartment. {ECO:0000269|PubMed:12644503}.
CC   -!- INDUCTION: Expression is sigma E-dependent.
CC       {ECO:0000269|PubMed:12644503}.
CC   -!- PTM: Three N-terminal lysines form epsilon-(gamma-glutamyl)lysine
CC       isopeptide bonds with glutamines of other spore coat proteins.
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DR   EMBL; X73124; CAA51618.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15818.1; -; Genomic_DNA.
DR   PIR; S39717; S39717.
DR   RefSeq; NP_391671.1; NC_000964.3.
DR   RefSeq; WP_003227448.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P39620; -.
DR   SMR; P39620; -.
DR   STRING; 224308.BSU37920; -.
DR   PaxDb; P39620; -.
DR   PRIDE; P39620; -.
DR   EnsemblBacteria; CAB15818; CAB15818; BSU_37920.
DR   GeneID; 937241; -.
DR   KEGG; bsu:BSU37920; -.
DR   PATRIC; fig|224308.179.peg.4106; -.
DR   eggNOG; ENOG5032T03; Bacteria.
DR   OMA; IAYTYPY; -.
DR   BioCyc; BSUB:BSU37920-MON; -.
DR   PRO; PR:P39620; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0031160; C:spore wall; IDA:UniProtKB.
DR   GO; GO:0018153; P:isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine; IMP:UniProtKB.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR014099; Spore_coat_GerQ.
DR   Pfam; PF09671; Spore_GerQ; 1.
DR   PIRSF; PIRSF038931; GerQ; 1.
DR   TIGRFAMs; TIGR02728; spore_gerQ; 1.
PE   1: Evidence at protein level;
KW   Germination; Isopeptide bond; Reference proteome; Sporulation.
FT   CHAIN           1..181
FT                   /note="Spore coat protein GerQ"
FT                   /id="PRO_0000049968"
FT   REGION          19..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        2
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-?)"
FT   CROSSLNK        4
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-?)"
FT   CROSSLNK        5
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-?)"
FT   MUTAGEN         1..5
FT                   /note="Missing: Eliminates cross-linking."
FT                   /evidence="ECO:0000269|PubMed:16936016"
FT   MUTAGEN         2
FT                   /note="K->A,Q: Cross-linking not affected. Cross-linking
FT                   not affected; when associated with A,Q-4 or A,Q-5. Cross-
FT                   linking eliminated, but still localizes CwlJ properly; when
FT                   associated with A,Q-4 and A,Q-5."
FT                   /evidence="ECO:0000269|PubMed:16936016"
FT   MUTAGEN         4
FT                   /note="K->A,Q: Cross-linking not affected. Cross-linking
FT                   not affected; when associated with A,Q-2 or A,Q-5. Cross-
FT                   linking eliminated, but still localizes CwlJ properly; when
FT                   associated with A,Q-2 and A,Q-5."
FT                   /evidence="ECO:0000269|PubMed:16936016"
FT   MUTAGEN         5
FT                   /note="K->A,Q: Cross-linking not affected. Cross-linking
FT                   not affected; when associated with A,Q-2 or A,Q-4. Cross-
FT                   linking eliminated, but still localizes CwlJ properly; when
FT                   associated with A,Q-2 and A,Q-4."
FT                   /evidence="ECO:0000269|PubMed:16936016"
SQ   SEQUENCE   181 AA;  20276 MW;  F8D88B4D8015C2F7 CRC64;
     MKPKKNQYQQ MQAFDNMQGY QPQFGANPYP QQGQGSQMQT MGMQPMMPMQ QGQQGQQGQQ
     GFGFPGQQQG GGFQIPSGPT PSGPGQSVPG MLPVEESYIE NILRLNRGKT ATIYMTFENS
     KEWGSKIFRG VIEAAGRDHI IISDPKSGTR YLLLTIYLDY ITFDEEIAYT YPYSMASYSP
     R
 
 
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