YCIC_BACSU
ID YCIC_BACSU Reviewed; 397 AA.
AC P94400; Q797P9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Putative metal chaperone YciC;
GN Name=yciC; OrderedLocusNames=BSU03360;
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=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
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 INDUCTION.
RX PubMed=9811636; DOI=10.1128/jb.180.22.5815-5821.1998;
RA Gaballa A., Helmann J.D.;
RT "Identification of a zinc-specific metalloregulatory protein, Zur,
RT controlling zinc transport operons in Bacillus subtilis.";
RL J. Bacteriol. 180:5815-5821(1998).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12426338; DOI=10.1128/jb.184.23.6508-6514.2002;
RA Gaballa A., Wang T., Ye R.W., Helmann J.D.;
RT "Functional analysis of the Bacillus subtilis Zur regulon.";
RL J. Bacteriol. 184:6508-6514(2002).
RN [5]
RP INDUCTION, AND PUTATIVE FUNCTION.
RX PubMed=18344368; DOI=10.1128/jb.01978-07;
RA Gabriel S.E., Miyagi F., Gaballa A., Helmann J.D.;
RT "Regulation of the Bacillus subtilis yciC gene and insights into the DNA-
RT binding specificity of the zinc-sensing metalloregulator Zur.";
RL J. Bacteriol. 190:3482-3488(2008).
RN [6]
RP INDUCTION.
RX PubMed=21821657; DOI=10.1093/nar/gkr625;
RA Ma Z., Gabriel S.E., Helmann J.D.;
RT "Sequential binding and sensing of Zn(II) by Bacillus subtilis Zur.";
RL Nucleic Acids Res. 39:9130-9138(2011).
CC -!- FUNCTION: May bind GTP. Might act as metal chaperone (Potential).
CC Contributes to optimal growth under starvation for zinc.
CC {ECO:0000269|PubMed:12426338, ECO:0000305}.
CC -!- INDUCTION: Repressed by zinc via the metallo-regulatory protein Zur.
CC {ECO:0000269|PubMed:18344368, ECO:0000269|PubMed:21821657,
CC ECO:0000269|PubMed:9811636}.
CC -!- DISRUPTION PHENOTYPE: No effect in wild-type, but required for optimal
CC growth in strains lacking the ZnuABC zinc uptake system.
CC {ECO:0000269|PubMed:12426338}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. CobW
CC subfamily. {ECO:0000305}.
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DR EMBL; D50453; BAA08970.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12130.1; -; Genomic_DNA.
DR PIR; B69760; B69760.
DR RefSeq; NP_388218.1; NC_000964.3.
DR RefSeq; WP_003234625.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P94400; -.
DR SMR; P94400; -.
DR IntAct; P94400; 1.
DR MINT; P94400; -.
DR STRING; 224308.BSU03360; -.
DR TCDB; 9.B.10.1.1; the putative tripartite zn(2+) transporter (tzt) family.
DR PaxDb; P94400; -.
DR PRIDE; P94400; -.
DR DNASU; 938322; -.
DR EnsemblBacteria; CAB12130; CAB12130; BSU_03360.
DR GeneID; 938322; -.
DR KEGG; bsu:BSU03360; -.
DR PATRIC; fig|224308.179.peg.351; -.
DR eggNOG; COG0523; Bacteria.
DR InParanoid; P94400; -.
DR OMA; WSQAGPN; -.
DR PhylomeDB; P94400; -.
DR BioCyc; BSUB:BSU03360-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1220.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011629; Cbl_biosynth_CobW-like_C.
DR InterPro; IPR036627; CobW-likC_sf.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR SMART; SM00833; CobW_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Chaperone; GTP-binding; Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..397
FT /note="Putative metal chaperone YciC"
FT /id="PRO_0000360621"
FT DOMAIN 259..374
FT /note="CobW C-terminal"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 73..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 183..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 397 AA; 45306 MW; AC9F293BC77B04BA CRC64;
MKKIPVTVLS GYLGAGKTTL LNSILQNREG LKIAVIVNDM SEVNIDAGLV KQEGGLSRTD
EKLVEMSNGC ICCTLREDLL IEVEKLAKDG RFDYIVIEST GISEPIPVAQ TFSYIDEEMG
IDLTKFCQLD TMVTVVDANR FWHDYQSGES LLDRKEALGE KDEREIADLL IDQIEFCDVL
ILNKCDLVSE QELEQLENVL RKLQPRARFI RSVKGNVKPQ EILHTGLFNF EEASGSAGWI
QELTAGHAEH TPETEEYGIS SFVYKRRLPF HSTRFYRWLD QMPKNVVRAK GIVWCASHNN
LALLMSQAGP SVTIEPVSYW VAALPKLEQE QVKQQEPEIL EEWDPEFGDR LTQLVFIGTD
LDEETITKEL DQCLLTEYEF DSDWSLFEDP FKWKLNQ
