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.
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; 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