YCLQ_BACSU
ID YCLQ_BACSU Reviewed; 317 AA.
AC P94421; Q797N9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Petrobactin-binding protein YclQ {ECO:0000305};
DE Flags: Precursor;
GN Name=yclQ; OrderedLocusNames=BSU03830;
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 PROTEIN SEQUENCE OF 30-40, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=10658653; DOI=10.1099/00221287-146-1-65;
RA Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT dimensional protein electrophoretic study.";
RL Microbiology 146:65-75(2000).
RN [4]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
RN [5] {ECO:0007744|PDB:3GFV}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 21-317, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=19955416; DOI=10.1073/pnas.0904793106;
RA Zawadzka A.M., Kim Y., Maltseva N., Nichiporuk R., Fan Y., Joachimiak A.,
RA Raymond K.N.;
RT "Characterization of a Bacillus subtilis transporter for petrobactin, an
RT anthrax stealth siderophore.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21854-21859(2009).
CC -!- FUNCTION: Part of the ABC transporter complex YclNOPQ involved in
CC uptake of ferric-petrobactin. Petrobactin is a photoreactive 3,4-
CC catecholate siderophore produced by many members of the B.cereus group,
CC including B.anthracis. Binds selectively iron-free and ferric
CC petrobactin and the petrobactin precursor 3,4-dihydroxybenzoic acid
CC (3,4-DHB). {ECO:0000269|PubMed:19955416}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (YclP),
CC two transmembrane proteins (YclN and YclO) and a solute-binding protein
CC (YclQ) (Probable). Interacts with FloT (PubMed:23651456).
CC {ECO:0000269|PubMed:23651456, ECO:0000305|PubMed:19955416}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:23651456}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Lipid-anchor. Note=Also found in the
CC extracellular protein fraction (PubMed:10658653). May exist in both
CC membrane-tethered and soluble form (Probable). Present in detergent-
CC resistant membrane (DRM) fractions that may be equivalent to eukaryotic
CC membrane rafts; these rafts include proteins involved in signaling,
CC molecule trafficking and protein secretion (PubMed:23651456).
CC {ECO:0000269|PubMed:10658653, ECO:0000269|PubMed:23651456,
CC ECO:0000305|PubMed:19955416}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutants are unable to use petrobactin
CC for iron delivery and growth. {ECO:0000269|PubMed:19955416}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
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DR EMBL; D50453; BAA09015.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12191.1; -; Genomic_DNA.
DR PIR; E69763; E69763.
DR RefSeq; NP_388265.1; NC_000964.3.
DR RefSeq; WP_003246619.1; NZ_JNCM01000031.1.
DR PDB; 3GFV; X-ray; 1.75 A; A/B=21-317.
DR PDBsum; 3GFV; -.
DR AlphaFoldDB; P94421; -.
DR SMR; P94421; -.
DR STRING; 224308.BSU03830; -.
DR PaxDb; P94421; -.
DR PRIDE; P94421; -.
DR DNASU; 938277; -.
DR EnsemblBacteria; CAB12191; CAB12191; BSU_03830.
DR GeneID; 938277; -.
DR KEGG; bsu:BSU03830; -.
DR PATRIC; fig|224308.179.peg.406; -.
DR eggNOG; COG4607; Bacteria.
DR InParanoid; P94421; -.
DR OMA; KMSAFGP; -.
DR PhylomeDB; P94421; -.
DR BioCyc; BSUB:BSU03830-MON; -.
DR EvolutionaryTrace; P94421; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR CDD; cd01140; FatB; 1.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR InterPro; IPR033870; FatB.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR PROSITE; PS50983; FE_B12_PBP; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Ion transport;
KW Iron; Iron transport; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..317
FT /note="Petrobactin-binding protein YclQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000359513"
FT DOMAIN 56..317
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 166..190
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:3GFV"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:3GFV"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:3GFV"
FT HELIX 301..316
FT /evidence="ECO:0007829|PDB:3GFV"
SQ SEQUENCE 317 AA; 34792 MW; 8F7588F466EED085 CRC64;
MKKFALLFIA LVTAVVISAC GNQSTSSKGS DTKKEQITVK HQLDKNGTKV PKNPKKVVVF
DFGSLDTLDK LGLDDIVAGL PKQVLPKYLS KFKDDKYADV GSLKEPDFDK VAELDPDLII
ISARQSESYK EFSKIAPTIY LGVDTAKYME SFKSDAETIG KIFDKEDKVK DELANIDHSI
ADVKKTAEKL NKNGLVIMAN DGKISAFGPK SRYGLIHDVF GVAPADQNIK ASTHGQSVSY
EYISKTNPDY LFVIDRGTAI GETSSTKQVV ENDYVKNVNA VKNGHVIYLD SATWYLSGGG
LESMTQMIKE VKDGLEK
