| Tag | Content |
|---|
| CPLM ID | CPLM-003054 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Succinyl-CoA ligase [ADP-forming] subunit beta |
Protein Synonyms/Alias | Succinyl-CoA synthetase subunit beta; SCS-beta |
Gene Name | sucC |
Gene Synonyms/Alias | b0728; JW0717 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 37 | EAEEAASKIGAGPWV | acetylation | [1, 2] | | 46 | GAGPWVVKCQVHAGG | acetylation | [2] | | 61 | RGKAGGVKVVNSKED | acetylation | [2] | | 66 | GVKVVNSKEDIRAFA | acetylation | [2] | | 79 | FAENWLGKRLVTYQT | acetylation | [2] | | 146 | ETPHLIHKVALDPLT | acetylation | [1, 2] | | 166 | QGRELAFKLGLEGKL | acetylation | [1, 2] | | 172 | FKLGLEGKLVQQFTK | acetylation | [1, 2] | | 205 | INPLVITKQGDLICL | acetylation | [1] | | 295 | DVGGGATKERVTEAF | acetylation | [2] | | 310 | KIILSDDKVKAVLVN | acetylation | [2] | | 359 | NNAELGAKKLADSGL | acetylation | [1, 2] | | 360 | NAELGAKKLADSGLN | acetylation | [1, 2] | | 372 | GLNIIAAKGLTDAAQ | acetylation | [1, 2] | | 388 | VVAAVEGK******* | acetylation | [1] |
|
Reference | [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | |
Sequence Annotation | DOMAIN 9 244 ATP-grasp.
NP_BIND 35 108 ATP (By similarity).
METAL 197 197 Magnesium or manganese (By similarity).
METAL 199 199 Magnesium or manganese (By similarity). |
Keyword | 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 388 AA |
Protein Sequence | MNLHEYQAKQ LFARYGLPAP VGYACTTPRE AEEAASKIGA GPWVVKCQVH AGGRGKAGGV 60
KVVNSKEDIR AFAENWLGKR LVTYQTDANG QPVNQILVEA ATDIAKELYL GAVVDRSSRR 120
VVFMASTEGG VEIEKVAEET PHLIHKVALD PLTGPMPYQG RELAFKLGLE GKLVQQFTKI 180
FMGLATIFLE RDLALIEINP LVITKQGDLI CLDGKLGADG NALFRQPDLR EMRDQSQEDP 240
REAQAAQWEL NYVALDGNIG CMVNGAGLAM GTMDIVKLHG GEPANFLDVG GGATKERVTE 300
AFKIILSDDK VKAVLVNIFG GIVRCDLIAD GIIGAVAEVG VNVPVVVRLE GNNAELGAKK 360
LADSGLNIIA AKGLTDAAQQ VVAAVEGK 388 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:UniProtKB. GO:0005524; F:ATP binding; IEA:HAMAP. GO:0000287; F:magnesium ion binding; IEA:HAMAP. GO:0030145; F:manganese ion binding; IEA:HAMAP. GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IMP:EcoliWiki. GO:0006099; P:tricarboxylic acid cycle; IMP:EcoliWiki. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |