(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 105.
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] {ECO:0000244|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). {ECO:0000305|PubMed:19955416}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC       Note=Also found in the extracellular protein fraction
CC       (PubMed:10658653). May exist in both membrane-tethered and soluble form
CC       (Probable). {ECO:0000269|PubMed:10658653, 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}.
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   SMR; P94421; -.
DR   STRING; 224308.BSU03830; -.
DR   PaxDb; P94421; -.
DR   PRIDE; P94421; -.
DR   EnsemblBacteria; CAB12191; CAB12191; BSU03830.
DR   GeneID; 938277; -.
DR   KEGG; bsu:BSU03830; -.
DR   PATRIC; fig|224308.179.peg.406; -.
DR   eggNOG; COG4607; LUCA.
DR   HOGENOM; HOG000099140; -.
DR   InParanoid; P94421; -.
DR   KO; K02016; -.
DR   OMA; KIAPTIY; -.
DR   PhylomeDB; P94421; -.
DR   BioCyc; BSUB:BSU03830-MONOMER; -.
DR   EvolutionaryTrace; P94421; -.
DR   Proteomes; UP000001570; Chromosome.
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;
DR   PRODOM; P94421.
DR   SWISS-2DPAGE; P94421.
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:0000244|PDB:3GFV"
FT   STRAND          44..53
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          57..59
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           62..70
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           74..76
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          77..80
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           87..93
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          97..99
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          103..106
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           108..113
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          117..121
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           123..128
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           129..135
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          138..140
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           145..147
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           148..162
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           166..190
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          193..200
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          203..207
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   TURN            212..214
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           215..218
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          223..225
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          236..238
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           240..246
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          249..255
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           256..260
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           266..270
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           273..275
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           279..282
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   STRAND          286..288
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           291..296
FT                   /evidence="ECO:0000244|PDB:3GFV"
FT   HELIX           301..316
FT                   /evidence="ECO:0000244|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
//

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