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Category: Protein modification

Name	Function
ctaG	formation of functional cytochrome C-oxidase (caa3)
defA	translation
lgt	lipomodification of lipoproteins
map	removal of N-terminal methionine from nascent proteins
yflG	removal of N-terminal methionine from nascent proteins

3.3.4.2. Protein kinases

Name	Function
bceS	resistance against toxic peptides
cheA	chemotactic signal modulator
citS	regulation of citrate uptake
comP	regulation of genetic competence and quorum sensing
cssS	control of cellular responses to protein secretion stress
dctS	regulation of the [gene\|9A96572B101358768EB20EE9438BE0E1424A4130\|dctS]-[gene\|97C34F6FA0B89D93369150E9A8AB3579332B07BC\|dctR]-[gene\|107DDCC7B6AA2D7CB02E53F043A93CF05C679081\|dctP] operon
degS	regulation of degradative enzyme and genetic competence
desK	regulation of cold shock expression of [gene\|644C0C354B72FC07222EE45F4D2E0E57434B5EB5\|des]
epsA	biofilm formation
epsB	biofilm formation
glnK	regulation of the [gene\|1A415DC85354373EA4866733C3AE43F510BD3C56\|glsA]-[gene\|E371BC4F613C40CB0E8C8CAA97387F3E6735D813\|glnT] operon
hprK	carbon catabolite repression,phosphorylation of [protein\|29B793660E4D30C0656248F3EF403FEF76FB9025\|HPr] and [protein\|A269774F2FDC94F93BA5F1360FFFE754B50383AD\|Crh] proteins at Ser46
kinA	initiation of sporulation
kinB	initiation of [SW\|sporulation]
kinC	initiation of [SW\|sporulation]
kinD	initiation of [SW\|sporulation]
kinE	initiation of [SW\|sporulation]
liaS	control of [protein\|49E70A20CC05DBE485953C0AE34E634EFB33C3B2\|LiaR] activity in response to bacitracin
lnrJ	involved in resistance to linearmycin
lytS	control of pyruvate utilization
malK	regulation of malate uptake
mcsB	control of [protein\|908DB17A39D518E84977250C55825E77FA02E391\|CtsR] activity
natK	regulation of the [gene\|B019FD0CB6F76C03DA5E76ABD1B324BA5E1A6936\|natA]-[gene\|A8ADA02BBB549866DE330040CF6D06ECC3B00099\|natB] operon
phoR	regulation of phosphate metabolism
prkA	control of [protein\|24F7FD5C7C3A68BB2760ABB8CBD8FBD65E5FF7D4\|SigK]-dependent gene expression
prkC	germination in response to muropeptides
prkD	unknown
psdS	resistance against toxic peptides
ptkA	protein phosphorylation
resE	regulation of aerobic and anaerobic respiration
rsbT	control of [protein\|580011DE5DC40EC9E7E0512791D328FAA010DCB8\|SigB] activity
rsbW	control of [protein\|search\|SigB ]activity
spoIIAB	control of [protein\|CFF318EE6CACDEE763FBF96A2ABB46E944679AAA\|SigF] activity; phosphorylation and inactivation of [protein\|3936E91C062074BFE4284B54A8CC33F35F94F5EE\|SpoIIAA]
tkmA	control of protein tyrosine phosphorylation
tsaE	control of tRNA modification
walK	control of cell wall metabolism
yabT	control of DNA integrity during spore development
ybdK	unknown
ycbM	unknown
yclK	unknown
ydfH	control of [gene\|1B61298ECA583D2112AA56A88358E8A9A55D2C9D\|ydfJ] expression
yesM	unknown
yhcY	unknown
ykoH	unknown
yrkQ	unknown
yvfT	unknown
yvrG	regulation cell surface maintenance
ywpD	unknown
yxdK	resistance against toxic peptides
yxjM	unknown

3.3.4.4. Protein phosphatases

Name	Function
cheC	motility and chemotaxis
fliY	movement and chemotaxis
prpC	antagonist of PrkC-dependent phosphorylation
prpE	unknown
ptpZ	protein tyrosine dephosphorylation
rapA	control of [SW\|sporulation] initiation
rapB	control of sporulation initiation
rapC	control of [protein\|search\|ComA ]activity
rapD	control of [protein\|7832489F11F606BCF637EC23BAAB41AD10237EBB\|ComA]-dependent gene expression
rapE	control of sporulation initiation
rapF	control of [protein\|7832489F11F606BCF637EC23BAAB41AD10237EBB\|ComA] activity
rapG	control of [protein\|D343D2096664A972026D911E7A17A35C7B1CD1C9\|DegU] activity
rapH	control of sporulation initiation and [protein\|7832489F11F606BCF637EC23BAAB41AD10237EBB\|ComA] activity
rapI	control of transfer of the mobile genetic element ICEBs1
rapJ	control of the [SW\|phosphorelay]
rapK	control of [protein\|search\|ComA ]activity
rsbP	control of [protein\|580011DE5DC40EC9E7E0512791D328FAA010DCB8\|SigB] activity
rsbU	control of [protein\|search\|SigB ]activity
rsbX	control of SigB activity
spo0E	initiation of sporulation
spoIIE	control of [protein\|search\|SigF ]activity, required for normal formation of the asymmetric septum
yfkJ	survival of stress conditions
yisI	control of [SW\|sporulation] initiation
ywlE	dephosphorylation of [protein\|7B1B664A1AE1F641E8E7D9E2894D5C8FFFA92948\|McsB]

3.3.4.5. Protein acetylases/ deacetylases

Name	Function
acuA	control of [protein\|search\|AcsA ]activity
acuC	control of [protein\|6671E7D85E99D349679F0E9D825DC035D10FFD2E\|AcsA] activity
srtN	control of [protein\|search\|AcsA ]activity
ydgE	unknown
yfmK	acetylation of the histone-like protein [protein\|EFD8FC875B6787B1512C5FC4C81E7E4C9BD93028\|HBsu], regulation of nucleoid compaction

important reviews

30967470,31091420

3.3.4.6. Protein acetylase/ deacetylase/ based on similarity

Name	Function
ydiD	unknown
yjcK	unknown
ynaD	unknown

3.3.4.7. Protein deaminase

Name	Function
cheD	[SW\|motility and chemotaxis]

3.3.4.8. Protein modification/ other

Name	Function
cheR	motility, chemotaxis
comQ	regulation of quorum sensing
gsaB	biosynthesis of heme, modification of [protein\|3054CD45713BBD69C2A528DE24AF6AF37175FD9D\|Efp]
pcp	removal of the N-terminal pyroglutamyl group from peptides
prmC	peptide release factor methylation
yaaO	control of [protein\|3054CD45713BBD69C2A528DE24AF6AF37175FD9D\|Efp] modification
yfkA	control of [protein\|3054CD45713BBD69C2A528DE24AF6AF37175FD9D\|Efp] modification
ymfI	modification of [protein\|3054CD45713BBD69C2A528DE24AF6AF37175FD9D\|Efp]
ynbB	modification of [protein\|3054CD45713BBD69C2A528DE24AF6AF37175FD9D\|Efp]
yolJ	biosynthesis of the antimicrobial peptide sublancin
yqeT	unknown
ywlG	control of [protein\|3054CD45713BBD69C2A528DE24AF6AF37175FD9D\|Efp] modification
yydG	control of [protein\|49E70A20CC05DBE485953C0AE34E634EFB33C3B2\|LiaR]-[protein\|9A1871BD853254EEA8B4E78CA187F9315CBDF43D\|LiaS] activity

key Reviews

21372323,20487279,25625314,25852656,30467398,30967470


3.3.1	Translation
3.3.2	Chaperones/ protein folding
3.3.3	Chaperone/ protein folding/ based on similarity
3.3.4	Protein modification
3.3.5	Protein secretion
3.3.6	Protein secretion/ based on similarity
3.3.7	Proteolysis