eF-site ID 1a3a-ABCD
PDB Code 1a3a
Chain A, B, C, D

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Title CRYSTAL STRUCTURE OF IIA MANNITOL FROM ESCHERICHIA COLI
Classification PHOSPHOTRANSFERASE
Compound MANNITOL-SPECIFIC EII
Source Escherichia coli (strain K12) (PTM3C_ECOLI)
Sequence A:  LFKLGAENIFLGRKAATKEEAIRFAGEQLVKGGYVEPEYV
QAMLDREKLTPTYLGESIAVPHGTVEAKDRVLKTGVVFCQ
YPEGVRFGEEEDDIARLVIGIAARNNEHIQVITSLTNALD
DESVIERLAHTTSVDEVLELLAGRK
B:  FKLGAENIFLGRKAATKEEAIRFAGEQLVKGGYVEPEYVQ
AMLDREKLTPTYLGESIAVPHGTVEAKDRVLKTGVVFCQY
PEGVRFGEEEDDIARLVIGIAARNNEHIQVITSLTNALDD
ESVIERLAHTTSVDEVLELLA
C:  NLFKLGAENIFLGRKAATKEEAIRFAGEQLVKGGYVEPEY
VQAMLDREKLTPTYLGESIAVPHGTVEAKDRVLKTGVVFC
QYPEGVRFGEEEDDIARLVIGIAARNNEHIQVITSLTNAL
DDESVIERLAHTTSVDEVLELLAGRK
D:  LFKLGAENIFLGRKAATKEEAIRFAGEQLVKGGYVEPEYV
QAMLDREKLTPTYLGESIAVPHGTVEAKDRVLKTGVVFCQ
YPEGVRFGEEEDDIARLVIGIAARNNEHIQVITSLTNALD
DESVIERLAHTTSVDEVLELLAGR
Description


Functional site

1) chain A
residue 65
type ACT_SITE
sequence H
description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00417, ECO:0000305|PubMed:12202490, ECO:0000305|PubMed:16443929, ECO:0000305|PubMed:9551558
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 65
type ACT_SITE
sequence H
description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00417, ECO:0000305|PubMed:12202490, ECO:0000305|PubMed:16443929, ECO:0000305|PubMed:9551558
source Swiss-Prot : SWS_FT_FI1

3) chain C
residue 65
type ACT_SITE
sequence H
description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00417, ECO:0000305|PubMed:12202490, ECO:0000305|PubMed:16443929, ECO:0000305|PubMed:9551558
source Swiss-Prot : SWS_FT_FI1

4) chain D
residue 65
type ACT_SITE
sequence H
description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00417, ECO:0000305|PubMed:12202490, ECO:0000305|PubMed:16443929, ECO:0000305|PubMed:9551558
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 49
type SITE
sequence R
description Stabilizes the transition state in the phosphoryl transfer from HPr to EIIA => ECO:0000269|PubMed:9551558
source Swiss-Prot : SWS_FT_FI2

6) chain B
residue 49
type SITE
sequence R
description Stabilizes the transition state in the phosphoryl transfer from HPr to EIIA => ECO:0000269|PubMed:9551558
source Swiss-Prot : SWS_FT_FI2

7) chain C
residue 49
type SITE
sequence R
description Stabilizes the transition state in the phosphoryl transfer from HPr to EIIA => ECO:0000269|PubMed:9551558
source Swiss-Prot : SWS_FT_FI2

8) chain D
residue 49
type SITE
sequence R
description Stabilizes the transition state in the phosphoryl transfer from HPr to EIIA => ECO:0000269|PubMed:9551558
source Swiss-Prot : SWS_FT_FI2

9) chain A
residue 65
type MOD_RES
sequence H
description Phosphohistidine; by HPr => ECO:0000269|PubMed:3142516, ECO:0000305|PubMed:12202490, ECO:0000305|PubMed:16443929, ECO:0000305|PubMed:2407724, ECO:0000305|PubMed:9551558
source Swiss-Prot : SWS_FT_FI3

10) chain B
residue 65
type MOD_RES
sequence H
description Phosphohistidine; by HPr => ECO:0000269|PubMed:3142516, ECO:0000305|PubMed:12202490, ECO:0000305|PubMed:16443929, ECO:0000305|PubMed:2407724, ECO:0000305|PubMed:9551558
source Swiss-Prot : SWS_FT_FI3

11) chain C
residue 65
type MOD_RES
sequence H
description Phosphohistidine; by HPr => ECO:0000269|PubMed:3142516, ECO:0000305|PubMed:12202490, ECO:0000305|PubMed:16443929, ECO:0000305|PubMed:2407724, ECO:0000305|PubMed:9551558
source Swiss-Prot : SWS_FT_FI3

12) chain D
residue 65
type MOD_RES
sequence H
description Phosphohistidine; by HPr => ECO:0000269|PubMed:3142516, ECO:0000305|PubMed:12202490, ECO:0000305|PubMed:16443929, ECO:0000305|PubMed:2407724, ECO:0000305|PubMed:9551558
source Swiss-Prot : SWS_FT_FI3

13) chain A
residue 50-66
type prosite
sequence EKLTPTYLGESIAVPHG
description PTS_EIIA_TYPE_2_HIS PTS EIIA domains phosphorylation site signature 2. EkltptyLGesIAVPHG
source prosite : PS00372


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