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Membrane-bound lytic murein transglycosylase F (EC 4.2.2.n1) (Murein lyase F)

 F4ASJ7_GLAS4            Unreviewed;       591 AA.
F4ASJ7;
28-JUN-2011, integrated into UniProtKB/TrEMBL.
28-JUN-2011, sequence version 1.
27-SEP-2017, entry version 49.
RecName: Full=Membrane-bound lytic murein transglycosylase F {ECO:0000256|HAMAP-Rule:MF_02016};
EC=4.2.2.n1 {ECO:0000256|HAMAP-Rule:MF_02016};
AltName: Full=Murein lyase F {ECO:0000256|HAMAP-Rule:MF_02016};
Flags: Precursor;
Name=mltF {ECO:0000256|HAMAP-Rule:MF_02016};
OrderedLocusNames=Glaag_1220 {ECO:0000313|EMBL:AEE22181.1};
Glaciecola sp. (strain 4H-3-7+YE-5).
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Alteromonadaceae; Glaciecola.
NCBI_TaxID=983545 {ECO:0000313|EMBL:AEE22181.1, ECO:0000313|Proteomes:UP000006544};
[1] {ECO:0000313|EMBL:AEE22181.1, ECO:0000313|Proteomes:UP000006544}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=4H-3-7+YE-5 {ECO:0000313|EMBL:AEE22181.1,
ECO:0000313|Proteomes:UP000006544};
PubMed=21705587; DOI=10.1128/JB.05468-11;
US DOE Joint Genome Institute;
Klippel B., Lochner A., Bruce D.C., Davenport K.W., Detter C.,
Goodwin L.A., Han J., Han S., Land M.L., Mikhailova N., Nolan M.,
Pennacchio L., Pitluck S., Tapia R., Woyke T., Wiebusch S., Basner A.,
Abe F., Horikoshi K., Keller M., Antranikian G.;
"Complete genome sequence of the marine, cellulose and xylan degrading
bacterium Glaciecola sp. 4H-3-7+YE-5.";
J. Bacteriol. 193:4547-4548(2011).
[2]
NUCLEOTIDE SEQUENCE.
STRAIN=4H-3-7+YE-5;
US DOE Joint Genome Institute;
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
Piela B., Lochner A., Antranikian F.I., Woyke T.;
"Complete sequence of chromosome of Glaciecola sp. 4H-3-7+YE-5.";
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Murein-degrading enzyme that degrades murein glycan
strands and insoluble, high-molecular weight murein sacculi, with
the concomitant formation of a 1,6-anhydromuramoyl product. Lytic
transglycosylases (LTs) play an integral role in the metabolism of
the peptidoglycan (PG) sacculus. Their lytic action creates space
within the PG sacculus to allow for its expansion as well as for
the insertion of various structures such as secretion systems and
flagella. {ECO:0000256|HAMAP-Rule:MF_02016,
ECO:0000256|SAAS:SAAS00176606}.
-!- CATALYTIC ACTIVITY: Exolytic cleavage of the (1->4)-beta-
glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-
acetylglucosamine (GlcNAc) residues in peptidoglycan, from either
the reducing or the non-reducing ends of the peptidoglycan chains,
with concomitant formation of a 1,6-anhydrobond in the MurNAc
residue. {ECO:0000256|HAMAP-Rule:MF_02016,
ECO:0000256|SAAS:SAAS00176617}.
-!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
Rule:MF_02016}; Peripheral membrane protein {ECO:0000256|HAMAP-
Rule:MF_02016}. Note=Attached to the inner leaflet of the outer
membrane. {ECO:0000256|HAMAP-Rule:MF_02016}.
-!- DOMAIN: The N-terminal domain does not have lytic activity and
probably modulates enzymatic activity. The C-terminal domain is
the catalytic active domain. {ECO:0000256|HAMAP-Rule:MF_02016}.
-!- SIMILARITY: In the C-terminal section; belongs to the
transglycosylase Slt family. {ECO:0000256|HAMAP-Rule:MF_02016,
ECO:0000256|SAAS:SAAS00539103}.
-!- SIMILARITY: In the N-terminal section; belongs to the bacterial
solute-binding protein 3 family. {ECO:0000256|HAMAP-Rule:MF_02016,
ECO:0000256|SAAS:SAAS00539112}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02016}.
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EMBL; CP002526; AEE22181.1; -; Genomic_DNA.
ProteinModelPortal; F4ASJ7; -.
STRING; 983545.Glaag_1220; -.
EnsemblBacteria; AEE22181; AEE22181; Glaag_1220.
KEGG; gag:Glaag_1220; -.
eggNOG; ENOG4105CHQ; Bacteria.
eggNOG; COG4623; LUCA.
KO; K18691; -.
OrthoDB; POG091H03Q9; -.
Proteomes; UP000006544; Chromosome.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:InterPro.
GO; GO:0008933; F:lytic transglycosylase activity; IEA:UniProtKB-UniRule.
GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniRule.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
HAMAP; MF_02016; MltF; 1.
InterPro; IPR023346; Lysozyme-like_dom.
InterPro; IPR023703; MltF.
InterPro; IPR001638; Solute-binding_3/MltF_N.
InterPro; IPR000189; Transglyc_AS.
InterPro; IPR008258; Transglycosylase_SLT_dom_1.
Pfam; PF00497; SBP_bac_3; 1.
Pfam; PF01464; SLT; 1.
SMART; SM00062; PBPb; 1.
SUPFAM; SSF53955; SSF53955; 1.
PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
3: Inferred from homology;
Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_02016,
ECO:0000256|SAAS:SAAS00176612};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02016,
ECO:0000256|SAAS:SAAS00176607};
Complete proteome {ECO:0000313|Proteomes:UP000006544};
Lyase {ECO:0000256|HAMAP-Rule:MF_02016,
ECO:0000256|SAAS:SAAS00176604};
Membrane {ECO:0000256|HAMAP-Rule:MF_02016,
ECO:0000256|SAAS:SAAS00176612};
Signal {ECO:0000256|HAMAP-Rule:MF_02016}.
SIGNAL 1 21 {ECO:0000256|HAMAP-Rule:MF_02016}.
CHAIN 22 591 Membrane-bound lytic murein
transglycosylase F. {ECO:0000256|HAMAP-
Rule:MF_02016}.
/FTId=PRO_5009011809.
DOMAIN 39 262 PBPb. {ECO:0000259|SMART:SM00062}.
REGION 263 591 LT domain. {ECO:0000256|HAMAP-
Rule:MF_02016}.
ACT_SITE 307 307 {ECO:0000256|HAMAP-Rule:MF_02016}.
SEQUENCE 591 AA; 66595 MW; 21EF8846B01E28FD CRC64;
MFFRWSFRYG FVLAVSLILS ACDEPKKQDS LQQVLDTGIL RVGTIYGLTT YYNGPNGPEG
FEYELAAGFA DYLGVKLEIF PYYTVNELFP QLDNAHFDVI AAGINVSPER YSQFRFGPAY
QNVSQKLVFK QGDVRPRELE DLTGNFMVVA GSGHSETLRN FKAEHPDLSW QETNDKDSEE
LLEAVLADEL DYTVVDSNIL ALMRRRYPEL SIGFSLSQSQ GIAWATSKKG DDALRAALIE
YFGKIHQNGT LAALEDKHFG HVRQFNYVDT RDFIRSAAEK LPQYQPLFEQ YANELDWRLL
AALSYQESHW NPKAKSVTGV RGLMMLTLNT AKDLGVTSRL DPEQSIRGGS EYLATLLTRI
PDRIPHPDRL WFALAAYNVG LGHLEDARVL TERQGGNPDM WVDVKKRLPQ LRQKRYYKTT
RYGYARGNEA VIYVDNIRRY YDTLVWLKEQ QPELMPVELQ EEQSDVQLGD VSGDNETEND
INERTSTPDA PKINGTKSET IEDKADGGDT VENATVENQT SQNAPSQKQT SKNETAQSQA
PETGPEQDKA GKNGASKNNA SDTPDAEKQA DSDSQPEESA DLLQDETNQE R


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