ID   MLTF_ALTMD              Reviewed;         463 AA.
AC   B4RVK5; F2G308;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 3.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Membrane-bound lytic murein transglycosylase F {ECO:0000255|HAMAP-Rule:MF_02016};
DE            EC=4.2.2.n1 {ECO:0000255|HAMAP-Rule:MF_02016};
DE   AltName: Full=Murein lyase F {ECO:0000255|HAMAP-Rule:MF_02016};
DE   Flags: Precursor;
GN   Name=mltF {ECO:0000255|HAMAP-Rule:MF_02016};
GN   OrderedLocusNames=MADE_1005430;
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(2008).
CC   -!- FUNCTION: Murein-degrading enzyme that degrades murein glycan strands
CC       and insoluble, high-molecular weight murein sacculi, with the
CC       concomitant formation of a 1,6-anhydromuramoyl product. Lytic
CC       transglycosylases (LTs) play an integral role in the metabolism of the
CC       peptidoglycan (PG) sacculus. Their lytic action creates space within
CC       the PG sacculus to allow for its expansion as well as for the insertion
CC       of various structures such as secretion systems and flagella.
CC       {ECO:0000255|HAMAP-Rule:MF_02016}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC         non-reducing ends of the peptidoglycan chains, with concomitant
CC         formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02016};
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane protein.
CC       Note=Attached to the inner leaflet of the outer membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_02016}.
CC   -!- DOMAIN: The N-terminal domain does not have lytic activity and probably
CC       modulates enzymatic activity. The C-terminal domain is the catalytic
CC       active domain. {ECO:0000255|HAMAP-Rule:MF_02016}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the bacterial solute-
CC       binding protein 3 family. {ECO:0000255|HAMAP-Rule:MF_02016}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transglycosylase
CC       Slt family. {ECO:0000255|HAMAP-Rule:MF_02016}.
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DR   EMBL; CP001103; AEA97232.2; -; Genomic_DNA.
DR   RefSeq; WP_020743009.1; NC_011138.3.
DR   AlphaFoldDB; B4RVK5; -.
DR   SMR; B4RVK5; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   PRIDE; B4RVK5; -.
DR   EnsemblBacteria; AEA97232; AEA97232; MADE_1005430.
DR   KEGG; amc:MADE_1005430; -.
DR   HOGENOM; CLU_027494_0_1_6; -.
DR   Proteomes; UP000001870; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:InterPro.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   HAMAP; MF_02016; MltF; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR023703; MltF.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   Pfam; PF01464; SLT; 1.
DR   SMART; SM00062; PBPb; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW   Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   CHAIN           34..463
FT                   /note="Membrane-bound lytic murein transglycosylase F"
FT                   /id="PRO_0000353920"
FT   REGION          34..272
FT                   /note="Non-LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   REGION          273..463
FT                   /note="LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   ACT_SITE        317
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ   SEQUENCE   463 AA;  52573 MW;  941DC3F6D2E5A082 CRC64;
     MQSQDYKKRL KLQIIIILSI AVMSCGVPNV PTALSSLLER ESIRVGTVYG AGTFYNGAEG
     PQGFEYELLA GFADYLGVTL DLYPFYSYEV MLEQLEEGNL DIVATGDAVT PALKRRFAYG
     PAYQRVEQEL VFQAGATRPR DLAELDSPII AVAGSSQAHL LSNLFKRLSE EEDEAVQTQL
     ITTEDSDSEE LLQQVANGDI AYTVADSNRL ALQRRRYPNL AVARTLNENM PMAWALPLQQ
     DDSVKAALIE YFGTVHQSGW FTVLEDKYFG HIRQFDYVDS RAFNYAAEST LTQYKSLFQK
     YAGDLDWRLL AAMSYQESHW NSDAISRTGV RGLMMLTLAT ASDWNVDDRT DPEQSIRGGS
     RYFASLLNRI PARISEPDRT WMAMASYNIG MGHLEDARIL TEQQGGNPDL WVDVKRRLPQ
     LRQKKYYRTT RYGYARGDEA LQYVENIRRY YDSLVWLDEQ GKI