ALBA_BACSU
ID ALBA_BACSU Reviewed; 448 AA.
AC P71011; Q8RKH6;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Antilisterial bacteriocin subtilosin biosynthesis protein AlbA;
DE EC=1.21.98.- {ECO:0000305|PubMed:22366720};
GN Name=albA; Synonyms=ywiA; OrderedLocusNames=BSU37370;
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=ATCC 6633 / PCI 219 / NRS 231;
RA Stein T., Duesterhus S., Entian K.-D.;
RT "Subtilosin A biosynthesis is conserved among two different classes of
RT Bacillus subtilis strains.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [3]
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 [4]
RP FUNCTION.
RC STRAIN=168 / JH642, and 22a;
RX PubMed=10572140; DOI=10.1128/jb.181.23.7346-7355.1999;
RA Zheng G., Yan L.Z., Vederas J.C., Zuber P.;
RT "Genes of the sbo-alb locus of Bacillus subtilis are required for
RT production of the antilisterial bacteriocin subtilosin.";
RL J. Bacteriol. 181:7346-7355(1999).
RN [5]
RP FUNCTION.
RC STRAIN=168 / JH642;
RX PubMed=10809709; DOI=10.1128/jb.182.11.3266-3273.2000;
RA Zheng G., Hehn R., Zuber P.;
RT "Mutational analysis of the sbo-alb locus of Bacillus subtilis:
RT identification of genes required for subtilosin production and immunity.";
RL J. Bacteriol. 182:3266-3273(2000).
RN [6]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=168 / JH642;
RX PubMed=10809710; DOI=10.1128/jb.182.11.3274-3277.2000;
RA Nakano M.M., Zheng G., Zuber P.;
RT "Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of
RT signal transduction under anaerobic conditions in Bacillus subtilis.";
RL J. Bacteriol. 182:3274-3277(2000).
RN [7]
RP FUNCTION, SUBSTRATE SPECIFICITY, POSSIBLE REACTION MECHANISM, COFACTOR,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 129-CYS--CYS-136 AND
RP 408-CYS--CYS-417.
RC STRAIN=168;
RX PubMed=22366720; DOI=10.1038/nchembio.798;
RA Fluehe L., Knappe T.A., Gattner M.J., Schaefer A., Burghaus O., Linne U.,
RA Marahiel M.A.;
RT "The radical SAM enzyme AlbA catalyzes thioether bond formation in
RT subtilosin A.";
RL Nat. Chem. Biol. 8:350-357(2012).
CC -!- FUNCTION: Catalyzes the formation of 3 thioether bonds during
CC production of the sactipeptide subtilosin from SboA. In vitro the
CC thioether bonds cannot be made in the absence of the SboA propeptide,
CC suggesting this is the first reaction in subtilosin maturation
CC (PubMed:22366720). In vitro, in the absence of a second substrate,
CC cleaves S-adenosyl-L-methionine into Met and 5'-dA (PubMed:22366720).
CC {ECO:0000269|PubMed:10572140, ECO:0000269|PubMed:10809709,
CC ECO:0000269|PubMed:22366720}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:22366720};
CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine, the other is
CC coordinated via 3 cysteines and maybe direct contact with the SboA
CC precursor. {ECO:0000269|PubMed:22366720};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22366720}.
CC -!- INDUCTION: Transcription is highly induced by oxygen limitation and is
CC under dual and independent control of Spo0A-AbrB and ResDE.
CC {ECO:0000269|PubMed:10809710}.
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DR EMBL; AJ430547; CAD23199.1; -; Genomic_DNA.
DR EMBL; Z80360; CAB02509.1; -; Genomic_DNA.
DR EMBL; Z97024; CAB09700.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15764.1; -; Genomic_DNA.
DR PIR; B70059; B70059.
DR RefSeq; NP_391617.1; NC_000964.3.
DR RefSeq; WP_003242599.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P71011; -.
DR SMR; P71011; -.
DR STRING; 224308.BSU37370; -.
DR jPOST; P71011; -.
DR PaxDb; P71011; -.
DR EnsemblBacteria; CAB15764; CAB15764; BSU_37370.
DR GeneID; 937059; -.
DR KEGG; bsu:BSU37370; -.
DR PATRIC; fig|224308.179.peg.4047; -.
DR eggNOG; COG0535; Bacteria.
DR InParanoid; P71011; -.
DR OMA; GWGRQFF; -.
DR PhylomeDB; P71011; -.
DR BioCyc; BSUB:BSU37370-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030152; P:bacteriocin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.1150; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR008792; PQQD.
DR InterPro; IPR041881; PqqD_sf.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF05402; PqqD; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Antibiotic biosynthesis; Bacteriocin biosynthesis; Cytoplasm; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..448
FT /note="Antilisterial bacteriocin subtilosin biosynthesis
FT protein AlbA"
FT /id="PRO_0000064542"
FT DOMAIN 115..329
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000269|PubMed:22366720"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000269|PubMed:22366720"
FT BINDING 136
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000269|PubMed:22366720"
FT BINDING 408
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-substrate"
FT /evidence="ECO:0000269|PubMed:22366720"
FT BINDING 414
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-substrate"
FT /evidence="ECO:0000269|PubMed:22366720"
FT BINDING 417
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-substrate"
FT /evidence="ECO:0000269|PubMed:22366720"
FT VARIANT 91
FT /note="Q -> L (in strain: ATCC 6633)"
FT VARIANT 96
FT /note="I -> V (in strain: ATCC 6633)"
FT VARIANT 99..108
FT /note="GNRASRHTIT -> ENQSTRHAIN (in strain: ATCC 6633)"
FT VARIANT 214
FT /note="T -> A (in strain: ATCC 6633)"
FT VARIANT 232
FT /note="V -> I (in strain: ATCC 6633)"
FT VARIANT 309
FT /note="D -> N (in strain: ATCC 6633)"
FT VARIANT 322..323
FT /note="HV -> NI (in strain: ATCC 6633)"
FT VARIANT 412
FT /note="G -> S (in strain: ATCC 6633)"
FT MUTAGEN 129..136
FT /note="CNLKCAHC->ANLKAAHA: No longer cleaves SAM, does not
FT make thioether bonds, contains 68% iron of wild-type."
FT /evidence="ECO:0000269|PubMed:22366720"
FT MUTAGEN 408..417
FT /note="CPFSGYCGGC->APFSGYAGGA: Weakly cleaves SAM but does
FT not make thioether bonds, contains 68% iron of wild-type."
FT /evidence="ECO:0000269|PubMed:22366720"
SQ SEQUENCE 448 AA; 51514 MW; DA3247604BC8CCAA CRC64;
MFIEQMFPFI NESVRVHQLP EGGVLEIDYL RDNVSISDFE YLDLNKTAYE LCMRMDGQKT
AEQILAEQCA VYDESPEDHK DWYYDMLNML QNKQVIQLGN RASRHTITTS GSNEFPMPLH
ATFELTHRCN LKCAHCYLES SPEALGTVSI EQFKKTADML FDNGVLTCEI TGGEIFVHPN
ANEILDYVCK KFKKVAVLTN GTLMRKESLE LLKTYKQKII VGISLDSVNS EVHDSFRGRK
GSFAQTCKTI KLLSDHGIFV RVAMSVFEKN MWEIHDMAQK VRDLGAKAFS YNWVDDFGRG
RDIVHPTKDA EQHRKFMEYE QHVIDEFKDL IPIIPYERKR AANCGAGWKS IVISPFGEVR
PCALFPKEFS LGNIFHDSYE SIFNSPLVHK LWQAQAPRFS EHCMKDKCPF SGYCGGCYLK
GLNSNKYHRK NICSWAKNEQ LEDVVQLI
