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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR1229 IGR1231 IGR1230 IGR1233 IGR1232 IGR1228 IGR1226 IGR1226.1 IGR1227 dpj, - NG1507 pdxJ, - NG1508 mutT, - NG1506 murI, - NG1500 NG1504 NG1498.1 NG1503 NG1499 amiC, - NG1502 dpj, - NG1507 pdxJ, - NG1508 mutT, - NG1506 murI, - NG1500 NG1504 NG1498.1 NG1503 NG1499 amiC, - NG1502 Type: tandem, Name:  - 69 dpj, - NG1507 pdxJ, - NG1508 mutT, - NG1506 murI, - NG1500 NG1504 NG1505 NG1505 NG1498.1 NG1503 NG1499 amiC, - NG1502 NG1501 NG1501
* Calculated from Protein Sequence

Gene ID: NG1502

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
amiC  

Definition:
N-acetylmuramoyl-L-alanine amidase

Gene Start:
1470322

Gene Stop:
1471617

Gene Length:
1296

Molecular Weight*:
46991

pI*:
11.00

Net Charge*:
22.37

EC:
3.5.1.28  

Functional Class:
Cell envelope; Murein sacculus and peptidoglycan  

Pathway: pathway table
Peptideglycan biosynthesis

Secondary Evidence:
Heidrich C, Templin MF, Ursinus A, Merdanovic M, Berger J, Schwarz H, de Pedro MA, Holtje JV.
Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli.
Mol Microbiol. 2001 Jul;41(1):167-78.
PMID: 11454209

Norman RA, Poh CL, Pearl LH, O'Hara BP, Drew RE.
Steric hindrance regulation of the Pseudomonas aeruginosa amidase operon.
J Biol Chem. 2000 Sep 29;275(39):30660-7.
PMID: 10893220

O'Hara BP, Norman RA, Wan PT, Roe SM, Barrett TE, Drew RE, Pearl LH.
Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated transcription antitermination complex.
EMBO J. 1999 Oct 1;18(19):5175-86.
PMID: 10508151

Comment:
Oklahoma ID: NGO.1502

Blast Summary:  PSI-Blast Search
Residues 17-432 in NG1502 have 98% similarity to residues 1-416 in AE002401, N. meningitidis MC58 N-acetylmuramoyl-L-alanine amidase.
Residues 39-427 in NG1502 have 40% similarity to residues 18-403 in AE004907, P. aeruginosa N-acetylmuramoyl-L-alanine amidase.
Residues 42-423 in NG1502 have 33% similarity to residues 27-398 in AE004123, V. cholerae N-acetylmuramoyl-L-alanine amidase.

COGS Summary:  COGS Search
BeTs to 9 clades of COG0860
COG name: N-acetylmuramoyl-L-alanine amidase
Functional Class:  M
The phylogenetic pattern of COG0860 is -----q-CEBRhuj--olin-
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB002508 (Cell wall hydrolase/autolysin) with a combined E-value of 3.3e-50.
    IPB002508A    210-222
    IPB002508B    225-248
    IPB002508C    275-284
    IPB002508D    374-413


ProDom Summary:  Protein Domain Search
Residues 276-346 are 59% similar to a (N-ACETYLMURAMOYL-L-ALANINE AMIDASE PRECURSOR HYDROLASE) protein domain (PD010743) which is seen in AMIC_ECOLI.

Residues 215-263 are 51% similar to a (AMIDASE N-ACETYLMURAMOYL-L-ALANINE) protein domain (PD003646) which is seen in P73105_SYNY3.

Residues 18-214 are 45% similar to a (N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC PRECURSOR EC) protein domain (PD106609) which is seen in AMIC_ECOLI.

Residues 348-423 are 55% similar to a (AMIDASE N-ACETYLMURAMOYL-L-ALANINE) protein domain (PD002984) which is seen in AMIC_ECOLI.



Paralogs:  Local Blast Search


NG1502 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 267 to 425 (E-value = 3.4e-76) place NG1502 in the Amidase_3 family which is described as N-acetylmuramoyl-L-alanine amidase (PF01520)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
75

PDB Hit:
No hits to the PDB database.

Gene Protein Sequence:
MPADRPYRTRTRKPAAMTKLTRRQIIRRTAGTLFALSPIASAVAKTVRAP
QFTAARIWPSHTYTRLTLESTAALKYQHFALDNPGRLVVDIQNANINTVL
HGLSQKVMADDPFIRSIRAGQNTPTTVRLVIDLKQPTHAQVFALPPVGGF
KDRLVVDLYPHGMDADDPMMALLNGSLNKTLRGSPEADPAQNTTPRPGRG
KNGRRPVIMLDPGHGGEDPGAVSPGGLQEKHVVLSIARETKKQLEALGYN
VFMTRNEDVFIPLGVRVAKGRARRADVFVSIHADAFTSPSARGTGVYMLN
TKGATSSAAKFLEQTQNNADAVGGVPTSGNRNVDTALLDMTQTATLRDSR
KLGKLVLEELGRLNHLHKGRVDEANFAVLRAPDMPSILVETAFLSNPAEE
KLLGSESFRRQCAQSIASGVQRYINTSVLKRG

Gene Nucleotide Sequence:  Sequence Viewer
ATGCCTGCTGACCGCCCATACCGAACGAGGACGCGAAAGCCTGCCGCTAT
GACCAAACTGACACGAAGACAAATCATCCGCCGCACCGCCGGCACACTGT
TCGCCCTGAGCCCCATCGCATCCGCCGTTGCCAAAACGGTACGCGCCCCG
CAGTTTACCGCCGCACGGATATGGCCGTCGCACACCTACACCCGCCTGAC
GCTGGAAAGCACCGCCGCGCTCAAATACCAGCACTTCGCGCTCGACAACC
CGGGCAGGTTGGTCGTCGATATACAAAACGCAAACATCAATACCGTATTG
CACGGGCTTTCCCAAAAAGTTATGGCGGACGACCCCTTTATCCGCAGCAT
ACGCGCGGGTCAGAACACGCCGACCACCGTCCGCCTCGTCATCGACCTGA
AACAGCCCACCCACGCACAAGTCTTCGCGCTTCCGCCCGTCGGCGGCTTT
AAGGACCGCCTCGTCGTCGACCTCTATCCGCACGGGATGGATGCCGACGA
TCCGATGATGGCGCTGCTCAACGGCAGCCTGAACAAAACCCTGCGCGGCT
CTCCGGAAGCCGACCCCGCCCAAAACACCACGCCCCGACCCGGGCGGGGC
AAAAACGGGCGCAGACCCGTCATCATGCTCGATCCGGGACACGGCGGTGA
AGACCCCGGCGCCGTCAGCCCGGGCGGTTTGCAGGAAAAACACGTCGTCC
TCTCCATCGCCCGCGAAACCAAAAAACAATTGGAAGCCTTGGGTTACAAC
GTCTTTATGACGCGCAACGAAGACGTGTTCATCCCATTGGGCGTGCGTGT
CGCCAAAGGGCGCGCACGGCGGGCGGACGTATTCGTCTCCATCCACGCCG
ACGCTTTCACCAGCCCCTCCGCGCGCGGAACGGGGGTTTATATGCTGAAC
ACCAAAGGCGCGACCAGCTCTGCCGCCAAATTCTTGGAACAAACCCAAAA
TAATGCCGACGCGGTCGGCGGCGTACCGACCAGCGGCAACCGCAACGTCG
ATACCGCCCTGCTCGACATGACGCAAACCGCCACACTGCGCGACAGCCGC
AAACTCGGCAAACTGGTGCTTGAAGAATTGGGCAGGCTCAACCATCTGCA
CAAAGGCAGGGTGGACGAAGCCAATTTCGCCGTATTGCGCGCACCCGATA
TGCCGTCTATCCTGGTCGAAACCGCCTTCCTGTCCAATCCTGCCGAAGAG
AAACTGCTGGGCAGCGAATCCTTCCGTCGGCAGTGCGCCCAATCCATTGC
CTCGGGTGTCCAACGCTACATCAATACATCCGTATTGAAGCGGGGT


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