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Protein

Surfactin synthase subunit 1

Gene

srfAA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains.

Cofactori

pantetheine 4'-phosphateNote: Binds 3 phosphopantetheines covalently.

Pathwayi: surfactin biosynthesis

This protein is involved in the pathway surfactin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway surfactin biosynthesis and in Antibiotic biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Antibiotic biosynthesis, Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU03480-MONOMER.
UniPathwayiUPA00181.

Names & Taxonomyi

Protein namesi
Recommended name:
Surfactin synthase subunit 1
Gene namesi
Name:srfAA
Synonyms:srfA, srfA1
Ordered Locus Names:BSU03480
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 35873587Surfactin synthase subunit 1PRO_0000193099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1006 – 10061O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication
Modified residuei2045 – 20451O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei3073 – 30731O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiP27206.

Interactioni

Protein-protein interaction databases

IntActiP27206. 4 interactions.
MINTiMINT-8364777.
STRINGi224308.Bsubs1_010100001948.

Structurei

3D structure databases

ProteinModelPortaliP27206.
SMRiP27206. Positions 4-438, 440-961, 964-1482, 1486-1999, 2005-2522, 2531-3027, 3033-3110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini976 – 104368Acyl carrier 1PROSITE-ProRule annotationAdd
BLAST
Domaini2015 – 208268Acyl carrier 2PROSITE-ProRule annotationAdd
BLAST
Domaini3043 – 310967Acyl carrier 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni? – 3114Domain 3 (D-leucine-activating)
Regioni? – 2086Domain 2 (leucine-activating)
Regioni? – 1047Domain 1 (glutamate-activating)

Sequence similaritiesi

Contains 3 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000229991.
InParanoidiP27206.
KOiK15654.
OMAiIPNRQHW.
PhylomeDBiP27206.

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR010060. NRPS_synth.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00501. AMP-binding. 3 hits.
PF13193. AMP-binding_C. 3 hits.
PF00668. Condensation. 4 hits.
PF00550. PP-binding. 3 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 3 hits.
TIGR01720. NRPS-para261. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00455. AMP_BINDING. 3 hits.
PS00012. PHOSPHOPANTETHEINE. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27206-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEITFYPLTD AQKRIWYTEK FYPHTSISNL AGIGKLVSAD AIDYVLVEQA
60 70 80 90 100
IQEFIRRNDA MRLRLRLDEN GEPVQYISEY RPVDIKHTDT TEDPNAIEFI
110 120 130 140 150
SQWSREETKK PLPLYDCDLF RFSLFTIKEN EVWFYANVHH VISDGISMNI
160 170 180 190 200
LGNAIMHIYL ELASGSETKE GISHSFIDHV LSEQEYAQSK RFEKDKAFWN
210 220 230 240 250
KQFESVPELV SLKRNASAGG SLDAERFSKD VPEALHQQIL SFCEANKVSV
260 270 280 290 300
LSVFQSLLAA YLYRVSGQND VVTGTFMGNR TNAKEKQMLG MFVSTVPLRT
310 320 330 340 350
NIDGGQAFSE FVKDRMKDLM KTLRHQKYPY NLLINDLRET KSSLTKLFTV
360 370 380 390 400
SLEYQVMQWQ KEEDLAFLTE PIFSGSGLND VSIHVKDRWD TGKLTIDFDY
410 420 430 440 450
RTDLFSREEI NMICERMITM LENALTHPEH TIDELTLISD AEKEKLLARA
460 470 480 490 500
GGKSVSYRKD MTIPELFQEK AELLSDHPAV VFEDRTLSYR TLHEQSARIA
510 520 530 540 550
NVLKQKGVGP DSPVAVLIER SERMITAIMG ILKAGGAYVP IDPGFPAERI
560 570 580 590 600
QYILEDCGAD FILTESKVAA PEADAELIDL DQAIEEGAEE SLNADVNARN
610 620 630 640 650
LAYIIYTSGT TGRPKGVMIE HRQVHHLVES LQQTIYQSGS QTLRMALLAP
660 670 680 690 700
FHFDASVKQI FASLLLGQTL YIVPKKTVTN GAALTAYYRK NSIEATDGTP
710 720 730 740 750
AHLQMLAAAG DFEGLKLKHM LIGGEGLSSV VADKLLKLFK EAGTAPRLTN
760 770 780 790 800
VYGPTETCVD ASVHPVIPEN AVQSAYVPIG KALGNNRLYI LDQKGRLQPE
810 820 830 840 850
GVAGELYIAG DGVGRGYLHL PELTEEKFLQ DPFVPGDRMY RTGDVVRWLP
860 870 880 890 900
DGTIEYLGRE DDQVKVRGYR IELGEIEAVI QQAPDVAKAV VLARPDEQGN
910 920 930 940 950
LEVCAYVVQK PGSEFAPAGL REHAARQLPD YMVPAYFTEV TEIPLTPSGK
960 970 980 990 1000
VDRRKLFALE VKAVSGTAYT APRNETEKAI AAIWQDVLNV EKAGIFDNFF
1010 1020 1030 1040 1050
ETGGHSLKAM TLLTKIHKET GIEIPLQFLF EHPTITALAE EADHRESKAF
1060 1070 1080 1090 1100
AVIEPAEKQE HYPLSLAQQR TYIVSQFEDA GVGYNMPAAA ILEGPLDIQK
1110 1120 1130 1140 1150
LERAFQGLIR RHESLRTSFV LENSTPRQKI HDSVDFNIEM IERGGRSDEA
1160 1170 1180 1190 1200
IMASFVRTFD LAKAPLFRIG LLGLEENRHM LLFDMHHLIS DGVSIGIMLE
1210 1220 1230 1240 1250
ELARIYKGEQ LPDLRLQYKD YAVWQSRQAA EGYKKDQAYW KEVFAGELPV
1260 1270 1280 1290 1300
LQLLSDYPRP PVQSFEGDRV SIKLDAGVKD RLNRLAEQNG ATLYMVMLSA
1310 1320 1330 1340 1350
YYTLLSKYTG QDDIIVGTPS AGRNHSDTEG IIGMFVNTLA IRSEVKQNET
1360 1370 1380 1390 1400
FTQLISRVRK RVLDAFSHQD YPFEWLVEDL NIPRDVSRHP LFDTMFSLQN
1410 1420 1430 1440 1450
ATEGIPAVGD LSLSVQETNF KIAKFDLTVQ ARETDEGIEI DVDYSTKLFK
1460 1470 1480 1490 1500
QSTADRLLTH FARLLEDAAA DPEKPISEYK LLSEEEAASQ IQQFNPGRTP
1510 1520 1530 1540 1550
YPKDKTIVQL FEEQAANTPD HTALQYEGES LTYRELNERA NRLARGILSL
1560 1570 1580 1590 1600
GAGEGRTAAV LCERSMDMIV SILAVLKSGS AYVPIDPEHP IQRMQHFFRD
1610 1620 1630 1640 1650
SGAKVLLTQR KLKALAEEAE FKGVIVLADE EESYHADARN LALPLDSAAM
1660 1670 1680 1690 1700
ANLTYTSGTT GTPKGNIVTH ANILRTVKET NYLSITEQDT ILGLSNYVFD
1710 1720 1730 1740 1750
AFMFDMFGSL LNGAKLVLIP KETVLDMARL SRVIERENIS ILMITTALFH
1760 1770 1780 1790 1800
LLVDLNPACL STLRKIMFGG ERASVEHVRK ALQTVGKGKL LHMYGPSEST
1810 1820 1830 1840 1850
VFATYHPVDE LEEHTLSVPI GKPVSNTEVY ILDRTGHVQP AGIAGELCVS
1860 1870 1880 1890 1900
GEGLVKGYYN RPELTEEKFV PHPFTSGERM YKTGDLARWL PNGDIEFIGR
1910 1920 1930 1940 1950
IDHQVKIRGQ RIELGEIEHQ LQTHDRVQES VVLAVDQGAG DKLLCAYYVG
1960 1970 1980 1990 2000
EGDISSQEMR EHAAKDLPAY MVPAVFIQMD ELPLTGNGKI DRRALPIPDA
2010 2020 2030 2040 2050
NVSRGVSYVA PRNGTEQKVA DIWAQVLQAE QVGAYDHFFD IGGHSLAGMK
2060 2070 2080 2090 2100
MLALVHQELG VELSLKDLFQ SPTVEGLAQV IASAEKGTAA SISPAEKQDT
2110 2120 2130 2140 2150
YPVSSPQKRM YVLQQLEDAQ TSYNMPAVLR LTGELDVERL NSVMQQLMQR
2160 2170 2180 2190 2200
HEALRTTFEI KDGETVQRIW EEAECEIAYF EAPEEETERI VSEFIKPFKI
2210 2220 2230 2240 2250
DQLPLFRIGL IKHSDTEHVL LFDMHHIISD GASVGVLIEE LSKLYDGETL
2260 2270 2280 2290 2300
EPLRIQYKDY AVWQQQFIQS ELYKKQEEHW LKELDGELPV LTLPTDYSRP
2310 2320 2330 2340 2350
AVQTFEGDRI AFSLEAGKAD ALRRLAKETD STLYMVLLAS YSAFLSKISG
2360 2370 2380 2390 2400
QDDIIVGSPV AGRSQADVSR VIGMFVNTLA LRTYPKGEKT FADYLNEVKE
2410 2420 2430 2440 2450
TALSAFDAQD YPLEDLIGNV QVQRDTSRNP LFDAVFSMQN ANIKDLTMKG
2460 2470 2480 2490 2500
IQLEPHPFER KTAKFDLTLT ADETDGGLTF VLEYNTALFK QETIERWKQY
2510 2520 2530 2540 2550
WMELLDAVTG NPNQPLSSLS LVTETEKQAL LEAWKGKALP VPTDKTVHQL
2560 2570 2580 2590 2600
FEETAQRHKD RPAVTYNGQS WTYGELNAKA NRLARILMDC GISPDDRVGV
2610 2620 2630 2640 2650
LTKPSLEMSA AVLGVLKAGA AFVPIDPDYP DQRIEYILQD SGAKLLLKQE
2660 2670 2680 2690 2700
GISVPDSYTG DVILLDGSRT ILSLPLDEND EENPETAVTA ENLAYMIYTS
2710 2720 2730 2740 2750
GTTGQPKGVM VEHHALVNLC FWHHDAFSMT AEDRSAKYAG FGFDASIWEM
2760 2770 2780 2790 2800
FPTWTIGAEL HVIEEAIRLD IVRLNDYFET NGVTITFLPT QLAEQFMELE
2810 2820 2830 2840 2850
NTSLRVLLTG GDKLKRAVKK PYTLVNNYGP TENTVVATSA EIHPEEGSLS
2860 2870 2880 2890 2900
IGRAIANTRV YILGEGNQVQ PEGVAGELCV AGRGLARGYL NREDETAKRF
2910 2920 2930 2940 2950
VADPFVPGER MYRTGDLVKW TGGGIEYIGR IDQQVKVRGY RIELSEIEVQ
2960 2970 2980 2990 3000
LAQLSEVQDA AVTAVKDKGG NTAIAAYVTP ESADIEALKS ALKETLPDYM
3010 3020 3030 3040 3050
IPAFWVTLNE LPVTANGKVD RKALPEPDIE AGSGEYKAPT TDMEELLAGI
3060 3070 3080 3090 3100
WQDVLGMSEV GVTDNFFSLG GDSIKGIQMA SRLNQHGWKL EMKDLFQHPT
3110 3120 3130 3140 3150
IEELTQYVER AEGKQADQGP VEGEVILTPI QRWFFEKNFT NKHHWNQSVM
3160 3170 3180 3190 3200
LHAKKGFDPE RVEKTLQALI EHHDALRMVY REGQEDVIQY NRGLEAASAQ
3210 3220 3230 3240 3250
LEVIQIEGQA ADYEDRIERE AERLQSSIDL QEGGLLKAGL FQAEDGDHLL
3260 3270 3280 3290 3300
LAIHHLVVDG VSWRILLEDF AAVYTQLEQG NEPVLPQKTH SFAEYAERLQ
3310 3320 3330 3340 3350
DFANSKAFLK EKEYWRQLEE QAVAAKLPKD RESGDQRMKH TKTIEFSLTA
3360 3370 3380 3390 3400
EETEQLTTKV HEAYHTEMND ILLTAFGLAM KEWTGQDRVS VHLEGHGREE
3410 3420 3430 3440 3450
IIEDLTISRT VGWFTSMYPM VLDMKHADDL GYQLKQMKED IRHVPNKGVG
3460 3470 3480 3490 3500
YGILRYLTAP EHKEDVAFSI QPDVSFNYLG QFDEMSDAGL FTRSELPSGQ
3510 3520 3530 3540 3550
SLSPETEKPN ALDVVGYIEN GKLTMSLAYH SLEFHEKTVQ TFSDSFKAHL
3560 3570 3580
LRIIEHCLSQ DGTELTPSDL GDDDLTLDEL DKLMEIF
Length:3,587
Mass (Da):402,146
Last modified:June 16, 2009 - v4
Checksum:i5CA8D98D71FD0A84
GO

Sequence cautioni

The sequence BAA08982 differs from that shown. Reason: Frameshift at positions 1065, 1085 and 1117. Curated
The sequence CAA49816 differs from that shown. Reason: Frameshift at positions 1065, 1085, 1093 and 1117. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461I → M in CAA49816 (PubMed:8355609).Curated
Sequence conflicti146 – 1461I → M in BAA08982 (PubMed:8969502).Curated
Sequence conflicti151 – 1511L → V in CAA49816 (PubMed:8355609).Curated
Sequence conflicti151 – 1511L → V in BAA08982 (PubMed:8969502).Curated
Sequence conflicti165 – 1651G → A in BAA02522 (PubMed:8441623).Curated
Sequence conflicti281 – 2811T → Q in CAA49816 (PubMed:8355609).Curated
Sequence conflicti281 – 2811T → Q in BAA08982 (PubMed:8969502).Curated
Sequence conflicti460 – 4601D → T in AAA22815 (PubMed:1847909).Curated
Sequence conflicti540 – 5401P → A in CAA49816 (PubMed:8355609).Curated
Sequence conflicti540 – 5401P → A in BAA08982 (PubMed:8969502).Curated
Sequence conflicti562 – 5621I → Y in CAA49816 (PubMed:8355609).Curated
Sequence conflicti562 – 5621I → Y in BAA08982 (PubMed:8969502).Curated
Sequence conflicti639 – 6402GS → PT in CAA49816 (PubMed:8355609).Curated
Sequence conflicti639 – 6402GS → PT in BAA08982 (PubMed:8969502).Curated
Sequence conflicti644 – 6441R → P in CAA49816 (PubMed:8355609).Curated
Sequence conflicti644 – 6441R → P in BAA08982 (PubMed:8969502).Curated
Sequence conflicti647 – 6493LLA → FLP in CAA49816 (PubMed:8355609).Curated
Sequence conflicti647 – 6493LLA → FLP in BAA08982 (PubMed:8969502).Curated
Sequence conflicti1026 – 10261L → Q in CAA49816 (PubMed:8355609).Curated
Sequence conflicti1026 – 10261L → Q in BAA08982 (PubMed:8969502).Curated
Sequence conflicti1132 – 11332DS → VC in CAA49816 (PubMed:8355609).Curated
Sequence conflicti1132 – 11332DS → VC in BAA08982 (PubMed:8969502).Curated
Sequence conflicti1164 – 11641A → R in BAA02522 (PubMed:8441623).Curated
Sequence conflicti1458 – 14581L → V in BAA02522 (PubMed:8441623).Curated
Sequence conflicti1850 – 18501S → T in CAA49816 (PubMed:8355609).Curated
Sequence conflicti1850 – 18501S → T in BAA08982 (PubMed:8969502).Curated
Sequence conflicti1894 – 18941D → T in CAA49816 (PubMed:8355609).Curated
Sequence conflicti1894 – 18941D → T in BAA08982 (PubMed:8969502).Curated
Sequence conflicti1911 – 19111R → A in CAA49816 (PubMed:8355609).Curated
Sequence conflicti1911 – 19111R → A in BAA08982 (PubMed:8969502).Curated
Sequence conflicti1973 – 19808PAVFIQMD → LRCLSKWT in BAA02522 (PubMed:8441623).Curated
Sequence conflicti2052 – 20521L → P in CAA49816 (PubMed:8355609).Curated
Sequence conflicti2052 – 20521L → P in BAA08982 (PubMed:8969502).Curated
Sequence conflicti2218 – 22181H → Q in CAA49816 (PubMed:8355609).Curated
Sequence conflicti2218 – 22181H → Q in BAA08982 (PubMed:8969502).Curated
Sequence conflicti2265 – 22662QQ → HR in CAA49816 (PubMed:8355609).Curated
Sequence conflicti2265 – 22662QQ → HR in BAA08982 (PubMed:8969502).Curated
Sequence conflicti2291 – 22911L → V in BAA02522 (PubMed:8441623).Curated
Sequence conflicti2349 – 23491S → C in CAA49816 (PubMed:8355609).Curated
Sequence conflicti2349 – 23491S → C in BAA08982 (PubMed:8969502).Curated
Sequence conflicti2428 – 24281R → S in CAA49816 (PubMed:8355609).Curated
Sequence conflicti2428 – 24281R → S in BAA08982 (PubMed:8969502).Curated
Sequence conflicti2611 – 26122AV → RC in BAA02522 (PubMed:8441623).Curated
Sequence conflicti2685 – 26851E → ENPE in CAA49816 (PubMed:8355609).Curated
Sequence conflicti2685 – 26851E → ENPE in BAA08982 (PubMed:8969502).Curated
Sequence conflicti2755 – 27551T → S in CAA49816 (PubMed:8355609).Curated
Sequence conflicti2755 – 27551T → S in BAA08982 (PubMed:8969502).Curated
Sequence conflicti2896 – 28972TA → SP in BAA02522 (PubMed:8441623).Curated
Sequence conflicti3025 – 30251P → N in CAA49816 (PubMed:8355609).Curated
Sequence conflicti3025 – 30251P → N in BAA08982 (PubMed:8969502).Curated
Sequence conflicti3096 – 30961F → N in CAA49816 (PubMed:8355609).Curated
Sequence conflicti3096 – 30961F → N in BAA08982 (PubMed:8969502).Curated
Sequence conflicti3271 – 32711A → S in CAA49816 (PubMed:8355609).Curated
Sequence conflicti3271 – 32711A → S in BAA08982 (PubMed:8969502).Curated
Sequence conflicti3316 – 33161R → S in CAA49816 (PubMed:8355609).Curated
Sequence conflicti3316 – 33161R → S in BAA08982 (PubMed:8969502).Curated
Sequence conflicti3451 – 34511Y → S in CAA49816 (PubMed:8355609).Curated
Sequence conflicti3451 – 34511Y → S in BAA08982 (PubMed:8969502).Curated
Sequence conflicti3483 – 349513DEMSD…FTRSE → HQMSHPPFFTTSH in CAA49816 (PubMed:8355609).CuratedAdd
BLAST
Sequence conflicti3483 – 349513DEMSD…FTRSE → HQMSHPPFFTTSH in BAA08982 (PubMed:8969502).CuratedAdd
BLAST
Sequence conflicti3499 – 35002GQ → PH in CAA49816 (PubMed:8355609).Curated
Sequence conflicti3499 – 35002GQ → PH in BAA08982 (PubMed:8969502).Curated
Sequence conflicti3507 – 35071E → R in BAA02522 (PubMed:8441623).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13262 Genomic DNA. Translation: BAA02522.1.
X70356 Genomic DNA. Translation: CAA49816.1. Frameshift.
D50453 Genomic DNA. Translation: BAA08982.1. Frameshift.
AL009126 Genomic DNA. Translation: CAB12142.2.
M59939 Genomic DNA. Translation: AAA22815.1.
D30762 Genomic DNA. Translation: BAA21034.1.
M64702 Genomic DNA. Translation: AAA22816.1.
PIRiI40485.
RefSeqiNP_388230.2. NC_000964.3.
WP_010886402.1. NZ_CP010052.1.

Genome annotation databases

EnsemblBacteriaiCAB12142; CAB12142; BSU03480.
GeneIDi938306.
KEGGibsu:BSU03480.
PATRICi18972261. VBIBacSub10457_0359.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13262 Genomic DNA. Translation: BAA02522.1.
X70356 Genomic DNA. Translation: CAA49816.1. Frameshift.
D50453 Genomic DNA. Translation: BAA08982.1. Frameshift.
AL009126 Genomic DNA. Translation: CAB12142.2.
M59939 Genomic DNA. Translation: AAA22815.1.
D30762 Genomic DNA. Translation: BAA21034.1.
M64702 Genomic DNA. Translation: AAA22816.1.
PIRiI40485.
RefSeqiNP_388230.2. NC_000964.3.
WP_010886402.1. NZ_CP010052.1.

3D structure databases

ProteinModelPortaliP27206.
SMRiP27206. Positions 4-438, 440-961, 964-1482, 1486-1999, 2005-2522, 2531-3027, 3033-3110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP27206. 4 interactions.
MINTiMINT-8364777.
STRINGi224308.Bsubs1_010100001948.

Proteomic databases

PaxDbiP27206.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12142; CAB12142; BSU03480.
GeneIDi938306.
KEGGibsu:BSU03480.
PATRICi18972261. VBIBacSub10457_0359.

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000229991.
InParanoidiP27206.
KOiK15654.
OMAiIPNRQHW.
PhylomeDBiP27206.

Enzyme and pathway databases

UniPathwayiUPA00181.
BioCyciBSUB:BSU03480-MONOMER.

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR010060. NRPS_synth.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00501. AMP-binding. 3 hits.
PF13193. AMP-binding_C. 3 hits.
PF00668. Condensation. 4 hits.
PF00550. PP-binding. 3 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 3 hits.
TIGR01720. NRPS-para261. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00455. AMP_BINDING. 3 hits.
PS00012. PHOSPHOPANTETHEINE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRFAA_BACSU
AccessioniPrimary (citable) accession number: P27206
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 16, 2009
Last modified: September 7, 2016
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The phosphoserine observed at Ser-1006 in PubMed:17218307 undoubtedly results from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.Curated

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.