Reviewed, UniProtKB/Swiss-Prot P53581 (AMPM3_SYNY3)

Names and origin

Protein names

Recommended name:
    Putative methionine aminopeptidase C
      Short name=MAP
    EC=3.4.11.18
Alternative name(s):
    Peptidase M

Gene names

Ordered Locus Names:

sll0555

Organism

Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins By similarity.
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Cofactor	Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity. Binds 1 sodium ion per subunit. The sodium ion has a structural role By similarity.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 305	305	Putative methionine aminopeptidase C		PRO_0000148965
Sites
	Metal binding	147	1	Cobalt 1 By similarity
	Metal binding	158	1	Cobalt 1 By similarity
	Metal binding	158	1	Cobalt 2 By similarity
	Metal binding	221	1	Cobalt 2 By similarity
	Metal binding	255	1	Cobalt 2 By similarity
	Metal binding	286	1	Cobalt 1 By similarity
	Metal binding	286	1	Cobalt 2 By similarity
	Binding site	129	1	Substrate By similarity
	Binding site	228	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P53581-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 69CCB51DD62EC0BE	FASTA	305	33,488
	10 20 30 40 50 60 MPRIFPWKLW RKSRPAWPRF LGTHPMNLLS QLFAPPSPVP SPTPKAKKRS RRGVQIKTPA 70 80 90 100 110 120 EIAIMRQAGA IAAQVLKEIA ATVQPGMTTG DLDQLAEERI RSLGATPSFK GYHGFPASIC 130 140 150 160 170 180 ACVNNEVVHG IPRRRKKIRS GDLLKVDTGA YFQGYHGDSC ITIAVGKVSP QAQRLMEVAE 190 200 210 220 230 240 GALYAGIEQV KPGNYLMDIA GAIEDYVKPT GYTIVEEFTG HGVGQALHED PHVFNVRCRD 250 260 270 280 290 300 LPNVKLKPGM TLAIEPIVNA GSRFTRTLGD RWTVVTVDNA LSAQFEHTVL VTATGYELLT DRRLV

References

[1]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed: 8590279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000022 Genomic DNA. Translation: BAA10478.1.
PIR	S75743.
RefSeq	NP_442408.2.
3D structure databases
HSSP	HSSP built from PDB template 1C24 based on UniProtKB P07906.
ModBase	Search...
Protein-protein interaction databases
IntAct	P53581. 1 interaction.
STRING	P53581.
Protein family/group databases
MEROPS	M24.001.
Genome annotation databases
GeneID	952411.
GenomeReviews	Gene locus sll0555 in contig BA000022_GR.
KEGG	syn:sll0555.
NMPDR	fig|1148.1.peg.2509.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P53581.
OMA	PATICTS.
Enzyme and pathway databases
BioCyc	SSP1148:SLL0555-MON.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
PANTHER	PTHR10804:SF13. Pept_M24A_MAP1. 1 hit. PTHR10804. Peptidase_M24_cat_core. 1 hit.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
TIGRFAMs	TIGR00500. met_pdase_I. 1 hit.
PROSITE	PS00680. MAP_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPM3_SYNY3

Accession

Primary (citable) accession number: P53581

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)