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Conserved domains on  [gi|1176170821|gb|OQX86366|]
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MAG: hypothetical protein B6D63_00040 [Candidatus Latescibacteria bacterium 4484_7]

Protein Classification

N-acetylmuramoyl-L-alanine amidase( domain architecture ID 12111088)

N-acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
161-395 3.07e-65

N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440621  Cd Length: 204  Bit Score: 208.58  E-value: 3.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 161 AKKKASAVARSGDYIVIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADKIDKyRGFRAVLTRKGDYNVSLQRRIDIAR 240
Cdd:COG0860    12 APAAARKGPPLKGKVIVIDPGHGGKDPGAIGPNGLKEKDVNLDIALRLAELLEA-PGAKVVLTRDDDTFVSLSERVAIAN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 241 SYGGDCFISLHMNSHYNKRARGSEVYYlslkgatdknaqavaekenlflemgdegtkfnddikeiiydLSRSNSMYKSSL 320
Cdd:COG0860    91 KAKADLFISIHANAAPNPSARGAEVYY-----------------------------------------YSGSQTSAESKK 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176170821 321 LAAEIASSLKRSRVLPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGVVSYLRK 395
Cdd:COG0860   130 LAEAIQKELVKALGLKDRGVKQANFYVLRETDMPAVLVELGFISNPEDEALLKSPAYQQKLAEAIADGILRYFGK 204
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 415-459 1.78e-13

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


:

Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 64.43  E-value: 1.78e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1176170821 415 TVHVVSKGETLWKIARRYKMRLQVLMDLNGLKKTGKIRPGQKLKV 459
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
AMIN pfam11741
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the ...
 51-149 1.20e-10

AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localizes to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localization of periplasmic protein complexes.


:

Pssm-ID: 463338  Cd Length: 96  Bit Score: 58.08  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821  51 IRFWTAPDHTRVVCDMSSESRYSIKTYSNPPKIAINIPGGRFARGVKGLVVNDGVIERIRINRLRSG-AQIVLDLKKPVE 129
Cdd:pfam11741   1 VRVWPTDDGTELELETSGGEKYQVFTLSNPNRLVIDIPGAQLGLPLKRIENPSPGIKSVRVGQFDPNtVRVVVDLDGSVL 80

                          90       100
                  ....*....|....*....|
gi 1176170821 130 FRdfalKPYKGRPHRIVIDV 149
Cdd:pfam11741  81 PQ----VPVFKSGEGLVVDL 96
 
Name Accession Description Interval E-value
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
161-395 3.07e-65

N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440621  Cd Length: 204  Bit Score: 208.58  E-value: 3.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 161 AKKKASAVARSGDYIVIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADKIDKyRGFRAVLTRKGDYNVSLQRRIDIAR 240
Cdd:COG0860    12 APAAARKGPPLKGKVIVIDPGHGGKDPGAIGPNGLKEKDVNLDIALRLAELLEA-PGAKVVLTRDDDTFVSLSERVAIAN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 241 SYGGDCFISLHMNSHYNKRARGSEVYYlslkgatdknaqavaekenlflemgdegtkfnddikeiiydLSRSNSMYKSSL 320
Cdd:COG0860    91 KAKADLFISIHANAAPNPSARGAEVYY-----------------------------------------YSGSQTSAESKK 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176170821 321 LAAEIASSLKRSRVLPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGVVSYLRK 395
Cdd:COG0860   130 LAEAIQKELVKALGLKDRGVKQANFYVLRETDMPAVLVELGFISNPEDEALLKSPAYQQKLAEAIADGILRYFGK 204
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 175-390 4.46e-59

N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.


Pssm-ID: 119407 [Multi-domain]  Cd Length: 172  Bit Score: 191.60  E-value: 4.46e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 175 IVIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADKIDKyRGFRAVLTRKGDYNVSLQRRIDIARSYGGDCFISLHMNS 254
Cdd:cd02696     1 TIVIDPGHGGKDPGAVGNDGLKEKDINLAIALKLAKLLEA-AGAKVVLTRDDDTFVSLSERVAIANRAGADLFISIHANA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 255 HYNKRARGSEVYYLslkgatdknaqavaekenlflemgdegtkfnddikeiiydlsrSNSMYKSSLLAAEIASSLKRSRV 334
Cdd:cd02696    80 APNSSARGAEVYYY-------------------------------------------SGSSEESKRLAEAIQKELVKALG 116

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1176170821 335 LPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGVV 390
Cdd:cd02696   117 LRNRGVKQANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPEYQDKIAEAIAEGIL 172
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
 176-389 7.79e-52

N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.


Pssm-ID: 426303  Cd Length: 174  Bit Score: 172.82  E-value: 7.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 176 VIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADKIDKYrGFRAVLTRKGDYNVSLQRRIDIARSYGGDCFISLHMNSH 255
Cdd:pfam01520   1 IVIDPGHGGKDPGAVGPNGILEKDINLKIALKLRKLLEAK-GAEVILTRDSDETVSLEERANIANSNGADLFVSIHANAF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 256 YNKRARGSEVYYLSLKGATDknaqavaekenlflemgdegtkfnddikeiiydlsrsnsmyKSSLLAAEIASSLKRSRVL 335
Cdd:pfam01520  80 PNSSASGVEVYYLAKRKSSA-----------------------------------------ESKRLAQSIQKELVKVLGL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1176170821 336 PFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGV 389
Cdd:pfam01520 119 KNRGVKPANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPAYQQKIAEAIADGI 172
PRK10319 PRK10319
N-acetylmuramoyl-L-alanine amidase AmiA;
140-393 1.88e-46

N-acetylmuramoyl-L-alanine amidase AmiA;


Pssm-ID: 182376 [Multi-domain]  Cd Length: 287  Bit Score: 162.25  E-value: 1.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 140 GRPHRIVIDVEKVLSSAEVQDAKKKASavarsGDYIVIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADkIDKYRGFR 219
Cdd:PRK10319   28 GMSQAIAKEEPLKTSNGHSKPKAKKSG-----GKRVVMLDPGHGGIDTGAIGRNGSKEKHVVLAIAKNVRS-ILRNHGID 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 220 AVLTRKGDYNVSLQRRIDIARSYGGDCFISLHMNSHYNKRARGSEVYYLSLKGATDKNAQAVAEKENLFLEMGdeGTKFN 299
Cdd:PRK10319  102 ARLTRSGDTFIPLYDRVEIAHKHGADLFMSIHADGFTNPKAAGASVFALSNRGASSAMAKYLSERENRADEVA--GKKAT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 300 DD---IKEIIYDLSRSNSMYKSSLLAAEIASSLKRSRVLPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTT 376
Cdd:PRK10319  180 DKdhlLQQVLFDLVQTDTIKNSLTLGSHILKKIKPVHKLHSRNTEQAAFVVLKSPSIPSVLVETSFITNPEEERLLGTTA 259

                         250
                  ....*....|....*..
gi 1176170821 377 TLKGLASAIAAGVVSYL 393
Cdd:PRK10319  260 FRQKIATAIAEGIISYF 276
spore_cwlD TIGR02883
N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of ...
 175-392 5.24e-30

N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]


Pssm-ID: 274337  Cd Length: 189  Bit Score: 115.11  E-value: 5.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 175 IVIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADKIDKyRGFRAVLTRKGDYNVS--------------LQRRIDIAR 240
Cdd:TIGR02883   2 IIVIDPGHGGIDGGAVGKDGTLEKDITLEIALKLKDYLQE-QGALVVMTREDDSDLAsegtkgysrrkiedLRKRVKLIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 241 SYGGDCFISLHMNSHYNKRARGSEVYYlslkgatdknaqavaekenlflemgdegtkfnddikeiiydlSRSNSmyKSSL 320
Cdd:TIGR02883  81 ESEADLFISIHLNAFPSSKYSGAQTFY------------------------------------------YGNSE--ENKR 116

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176170821 321 LAAEIASSLKRSRVLPFRSIKQANFV-VLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGVVSY 392
Cdd:TIGR02883 117 LAKFIQDELRRNLDNTNRRAKKINDYyLLRNAEVPGVIVECGFLSNPEEAELLKDEDYQQKIAAAIYKGVLRY 189
Ami_3 smart00646
Ami_3 domain;
237-389 5.45e-21

Ami_3 domain;


Pssm-ID: 214762  Cd Length: 113  Bit Score: 87.73  E-value: 5.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821  237 DIARSYGGDCFISLHMNSHYNKRARGSEVYYLSLKGAtdknaqavaekenlflemgdegtkfnddikeiiydlsrsnsMY 316
Cdd:smart00646   2 NIANAAKADLFVSIHANAGGASAARGFEVYYYSDKGA-----------------------------------------IR 40

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176170821  317 KSSLLAAEIASSLKRSRVLPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGV 389
Cdd:smart00646  41 ESRALASIIQKSLRKNTGLRDRGVKEANFAVLRETNMPAVLVELGFITNPSDARKLKSAAYQQKLARAIAKGI 113
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 415-459 1.78e-13

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 64.43  E-value: 1.78e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1176170821 415 TVHVVSKGETLWKIARRYKMRLQVLMDLNGLKKTGKIRPGQKLKV 459
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
417-459 8.00e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 62.46  E-value: 8.00e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1176170821  417 HVVSKGETLWKIARRYKMRLQVLMDLNGLKKTGKIRPGQKLKV 459
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 417-459 3.44e-12

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 60.87  E-value: 3.44e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1176170821 417 HVVSKGETLWKIARRYKMRLQVLMDLNGLkKTGKIRPGQKLKV 459
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGL-SSPNLYVGQKLKI 42
AMIN pfam11741
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the ...
 51-149 1.20e-10

AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localizes to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localization of periplasmic protein complexes.


Pssm-ID: 463338  Cd Length: 96  Bit Score: 58.08  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821  51 IRFWTAPDHTRVVCDMSSESRYSIKTYSNPPKIAINIPGGRFARGVKGLVVNDGVIERIRINRLRSG-AQIVLDLKKPVE 129
Cdd:pfam11741   1 VRVWPTDDGTELELETSGGEKYQVFTLSNPNRLVIDIPGAQLGLPLKRIENPSPGIKSVRVGQFDPNtVRVVVDLDGSVL 80

                          90       100
                  ....*....|....*....|
gi 1176170821 130 FRdfalKPYKGRPHRIVIDV 149
Cdd:pfam11741  81 PQ----VPVFKSGEGLVVDL 96
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 415-459 4.11e-07

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 49.62  E-value: 4.11e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1176170821 415 TVHVVSKGETLWKIARRY---KMRLQVLMDLN--GLKKTGKIRPGQKLKV 459
Cdd:COG1652   110 KTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPDLIYPGQVLRI 159
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
396-459 7.49e-06

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 48.54  E-value: 7.49e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1176170821 396 GGSVDDMTEQGDKADRKRITVHVVSKGETLWKIARRYKMRLQVLMDLNGLkKTGKIRPGQKLKV 459
Cdd:PRK06347  312 SGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNL-KSDFIYPGQKLKV 374
 
Name Accession Description Interval E-value
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
161-395 3.07e-65

N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440621  Cd Length: 204  Bit Score: 208.58  E-value: 3.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 161 AKKKASAVARSGDYIVIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADKIDKyRGFRAVLTRKGDYNVSLQRRIDIAR 240
Cdd:COG0860    12 APAAARKGPPLKGKVIVIDPGHGGKDPGAIGPNGLKEKDVNLDIALRLAELLEA-PGAKVVLTRDDDTFVSLSERVAIAN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 241 SYGGDCFISLHMNSHYNKRARGSEVYYlslkgatdknaqavaekenlflemgdegtkfnddikeiiydLSRSNSMYKSSL 320
Cdd:COG0860    91 KAKADLFISIHANAAPNPSARGAEVYY-----------------------------------------YSGSQTSAESKK 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176170821 321 LAAEIASSLKRSRVLPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGVVSYLRK 395
Cdd:COG0860   130 LAEAIQKELVKALGLKDRGVKQANFYVLRETDMPAVLVELGFISNPEDEALLKSPAYQQKLAEAIADGILRYFGK 204
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 175-390 4.46e-59

N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.


Pssm-ID: 119407 [Multi-domain]  Cd Length: 172  Bit Score: 191.60  E-value: 4.46e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 175 IVIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADKIDKyRGFRAVLTRKGDYNVSLQRRIDIARSYGGDCFISLHMNS 254
Cdd:cd02696     1 TIVIDPGHGGKDPGAVGNDGLKEKDINLAIALKLAKLLEA-AGAKVVLTRDDDTFVSLSERVAIANRAGADLFISIHANA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 255 HYNKRARGSEVYYLslkgatdknaqavaekenlflemgdegtkfnddikeiiydlsrSNSMYKSSLLAAEIASSLKRSRV 334
Cdd:cd02696    80 APNSSARGAEVYYY-------------------------------------------SGSSEESKRLAEAIQKELVKALG 116

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1176170821 335 LPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGVV 390
Cdd:cd02696   117 LRNRGVKQANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPEYQDKIAEAIAEGIL 172
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
 176-389 7.79e-52

N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.


Pssm-ID: 426303  Cd Length: 174  Bit Score: 172.82  E-value: 7.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 176 VIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADKIDKYrGFRAVLTRKGDYNVSLQRRIDIARSYGGDCFISLHMNSH 255
Cdd:pfam01520   1 IVIDPGHGGKDPGAVGPNGILEKDINLKIALKLRKLLEAK-GAEVILTRDSDETVSLEERANIANSNGADLFVSIHANAF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 256 YNKRARGSEVYYLSLKGATDknaqavaekenlflemgdegtkfnddikeiiydlsrsnsmyKSSLLAAEIASSLKRSRVL 335
Cdd:pfam01520  80 PNSSASGVEVYYLAKRKSSA-----------------------------------------ESKRLAQSIQKELVKVLGL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1176170821 336 PFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGV 389
Cdd:pfam01520 119 KNRGVKPANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPAYQQKIAEAIADGI 172
PRK10319 PRK10319
N-acetylmuramoyl-L-alanine amidase AmiA;
140-393 1.88e-46

N-acetylmuramoyl-L-alanine amidase AmiA;


Pssm-ID: 182376 [Multi-domain]  Cd Length: 287  Bit Score: 162.25  E-value: 1.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 140 GRPHRIVIDVEKVLSSAEVQDAKKKASavarsGDYIVIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADkIDKYRGFR 219
Cdd:PRK10319   28 GMSQAIAKEEPLKTSNGHSKPKAKKSG-----GKRVVMLDPGHGGIDTGAIGRNGSKEKHVVLAIAKNVRS-ILRNHGID 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 220 AVLTRKGDYNVSLQRRIDIARSYGGDCFISLHMNSHYNKRARGSEVYYLSLKGATDKNAQAVAEKENLFLEMGdeGTKFN 299
Cdd:PRK10319  102 ARLTRSGDTFIPLYDRVEIAHKHGADLFMSIHADGFTNPKAAGASVFALSNRGASSAMAKYLSERENRADEVA--GKKAT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 300 DD---IKEIIYDLSRSNSMYKSSLLAAEIASSLKRSRVLPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTT 376
Cdd:PRK10319  180 DKdhlLQQVLFDLVQTDTIKNSLTLGSHILKKIKPVHKLHSRNTEQAAFVVLKSPSIPSVLVETSFITNPEEERLLGTTA 259

                         250
                  ....*....|....*..
gi 1176170821 377 TLKGLASAIAAGVVSYL 393
Cdd:PRK10319  260 FRQKIATAIAEGIISYF 276
PRK10431 PRK10431
N-acetylmuramoyl-l-alanine amidase II; Provisional
 134-392 5.01e-35

N-acetylmuramoyl-l-alanine amidase II; Provisional


Pssm-ID: 236692 [Multi-domain]  Cd Length: 445  Bit Score: 135.37  E-value: 5.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 134 ALKPYKGRPHRIVIdvekVLSSAEVqdAKKKASAVARSGDYIVI-IDPGHGGSDPGAISRNGLREKDVVLRLAHLVADKI 212
Cdd:PRK10431  157 ARNPFKTESNRTTG----VISSNTV--TRPAARATANTGDKVIIaIDAGHGGQDPGAIGPGGTREKNVTIAIARKLRTLL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 213 DKYRGFRAVLTRKGDYNVSLQRRIDIARSYGGDCFISLHMNSHYNKRARGSEVYYLSLKGATDKNAQAVAEKENLFLEMG 292
Cdd:PRK10431  231 NDDPMFKGVLTRDGDYFISVMGRSDVARKQNANFLVSIHADAAPNRSATGASVWVLSNRRANSEMASWLEQHEKQSELLG 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 293 DEG-----TKFNDDIKEIIYDLSRSNSMYKSSLLAAEIASSLKRSRVLPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRR 367
Cdd:PRK10431  311 GAGdvlanSQSDPYLSQAVLDLQFGHSQRVGYDVATSVLSQLQRIGELHKRRPEHASLGVLRSPDIPSVLVETGFISNNS 390

                         250       260
                  ....*....|....*....|....*
gi 1176170821 368 DEKMIRKTTTLKGLASAIAAGVVSY 392
Cdd:PRK10431  391 EERLLASDDYQQQIAEAIYKGLRNY 415
spore_cwlD TIGR02883
N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of ...
 175-392 5.24e-30

N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]


Pssm-ID: 274337  Cd Length: 189  Bit Score: 115.11  E-value: 5.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 175 IVIIDPGHGGSDPGAISRNGLREKDVVLRLAHLVADKIDKyRGFRAVLTRKGDYNVS--------------LQRRIDIAR 240
Cdd:TIGR02883   2 IIVIDPGHGGIDGGAVGKDGTLEKDITLEIALKLKDYLQE-QGALVVMTREDDSDLAsegtkgysrrkiedLRKRVKLIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 241 SYGGDCFISLHMNSHYNKRARGSEVYYlslkgatdknaqavaekenlflemgdegtkfnddikeiiydlSRSNSmyKSSL 320
Cdd:TIGR02883  81 ESEADLFISIHLNAFPSSKYSGAQTFY------------------------------------------YGNSE--ENKR 116

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176170821 321 LAAEIASSLKRSRVLPFRSIKQANFV-VLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGVVSY 392
Cdd:TIGR02883 117 LAKFIQDELRRNLDNTNRRAKKINDYyLLRNAEVPGVIVECGFLSNPEEAELLKDEDYQQKIAAAIYKGVLRY 189
Ami_3 smart00646
Ami_3 domain;
237-389 5.45e-21

Ami_3 domain;


Pssm-ID: 214762  Cd Length: 113  Bit Score: 87.73  E-value: 5.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821  237 DIARSYGGDCFISLHMNSHYNKRARGSEVYYLSLKGAtdknaqavaekenlflemgdegtkfnddikeiiydlsrsnsMY 316
Cdd:smart00646   2 NIANAAKADLFVSIHANAGGASAARGFEVYYYSDKGA-----------------------------------------IR 40

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176170821  317 KSSLLAAEIASSLKRSRVLPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGV 389
Cdd:smart00646  41 ESRALASIIQKSLRKNTGLRDRGVKEANFAVLRETNMPAVLVELGFITNPSDARKLKSAAYQQKLARAIAKGI 113
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 415-459 1.78e-13

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 64.43  E-value: 1.78e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1176170821 415 TVHVVSKGETLWKIARRYKMRLQVLMDLNGLKKTGKIRPGQKLKV 459
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
321-461 2.14e-13

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 67.81  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 321 LAAEIASSLKRSRVLPFRSIKQANFVVLRSVAVPSVLVEAAFLSNRRDEKMIRKTTTLKGLASAIAAGVVSYLRKGGSVD 400
Cdd:COG1388    16 VLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLS 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176170821 401 DMTEQGDKADRKRITVHVVSKGETLWKIARRYKMRLQVLMDLNGLKKTgKIRPGQKLKVYR 461
Cdd:COG1388    96 GIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSD-TIRPGQKLKIPA 155
LysM smart00257
Lysin motif;
417-459 8.00e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 62.46  E-value: 8.00e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1176170821  417 HVVSKGETLWKIARRYKMRLQVLMDLNGLKKTGKIRPGQKLKV 459
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 417-459 3.44e-12

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 60.87  E-value: 3.44e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1176170821 417 HVVSKGETLWKIARRYKMRLQVLMDLNGLkKTGKIRPGQKLKV 459
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGL-SSPNLYVGQKLKI 42
AMIN pfam11741
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the ...
 51-149 1.20e-10

AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localizes to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localization of periplasmic protein complexes.


Pssm-ID: 463338  Cd Length: 96  Bit Score: 58.08  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821  51 IRFWTAPDHTRVVCDMSSESRYSIKTYSNPPKIAINIPGGRFARGVKGLVVNDGVIERIRINRLRSG-AQIVLDLKKPVE 129
Cdd:pfam11741   1 VRVWPTDDGTELELETSGGEKYQVFTLSNPNRLVIDIPGAQLGLPLKRIENPSPGIKSVRVGQFDPNtVRVVVDLDGSVL 80

                          90       100
                  ....*....|....*....|
gi 1176170821 130 FRdfalKPYKGRPHRIVIDV 149
Cdd:pfam11741  81 PQ----VPVFKSGEGLVVDL 96
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 415-459 4.11e-07

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 49.62  E-value: 4.11e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1176170821 415 TVHVVSKGETLWKIARRY---KMRLQVLMDLN--GLKKTGKIRPGQKLKV 459
Cdd:COG1652   110 KTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPDLIYPGQVLRI 159
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
396-459 7.49e-06

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 48.54  E-value: 7.49e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1176170821 396 GGSVDDMTEQGDKADRKRITVHVVSKGETLWKIARRYKMRLQVLMDLNGLkKTGKIRPGQKLKV 459
Cdd:PRK06347  312 SGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNL-KSDFIYPGQKLKV 374
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
416-459 2.75e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 46.61  E-value: 2.75e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1176170821 416 VHVVSKGETLWKIARRYKMRLQVLMDLNGLkKTGKIRPGQKLKV 459
Cdd:PRK06347  481 VYTVAKGDSLWRIANNNKVTIANLKSWNNL-KSDFIYPGQKLKV 523
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
416-459 3.93e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 46.23  E-value: 3.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1176170821 416 VHVVSKGETLWKIARRYKMRLQVLMDLNGLkKTGKIRPGQKLKV 459
Cdd:PRK06347  407 VYTVVKGDSLWRIANNNKVTIANLKSWNNL-KSDFIYPGQKLKV 449
AMIN pfam11741
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the ...
 109-170 6.56e-04

AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localizes to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localization of periplasmic protein complexes.


Pssm-ID: 463338  Cd Length: 96  Bit Score: 38.82  E-value: 6.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176170821 109 IRINRLRSGAQIVLDLKKPVEFRDFALKpykgRPHRIVIDVEKVLSSAEVQDAKKKASAVAR 170
Cdd:pfam11741   1 VRVWPTDDGTELELETSGGEKYQVFTLS----NPNRLVIDIPGAQLGLPLKRIENPSPGIKS 58
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
405-459 1.10e-03

Putative Zn-dependent protease [General function prediction only];


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 405 QGDKADRK--RITVHVVSKGETLWKIARRYKM---RLQVLMDLNGLKKTGKIRPGQKLKV 459
Cdd:COG4784   427 DAEAAALKplRIRVVTVKPGDTVASLAARMPVpdrPEERFRLLNGLYPGGELKPGQLVKI 486
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 375-459 1.42e-03

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 39.13  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176170821 375 TTTLKGLASA--------IAAGVVSYLrkgGSVDD--MTEQGDKADRkritVHVVSKGETLWKIARRY---KMRLQVLMD 441
Cdd:PRK11198   53 KATVSGDAASqeakekilLAVGNIQGI---ASVDDqvKVATPAPESQ----FYTVKSGDTLSAIAKKVygnANKYNKIFE 125

                          90       100
                  ....*....|....*....|
gi 1176170821 442 LNG--LKKTGKIRPGQKLKV 459
Cdd:PRK11198  126 ANKpmLKSPDKIYPGQVLRI 145
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 419-459 5.19e-03

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 38.95  E-value: 5.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1176170821 419 VSKGETLWKIARRYKMRLQVLMDLNGLkKTGKIRPGQKLKV 459
Cdd:PRK10783  348 VRSGDTLSGIASRLNVSTKDLQQWNNL-RGSKLKVGQTLTI 387
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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