ID   MLTF_CITK8              Reviewed;         515 AA.
AC   A8AD27;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-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}; OrderedLocusNames=CKO_00225;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV11390.1; -; Genomic_DNA.
DR   RefSeq; WP_012131223.1; NC_009792.1.
DR   AlphaFoldDB; A8AD27; -.
DR   SMR; A8AD27; -.
DR   STRING; 290338.CKO_00225; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; ABV11390; ABV11390; CKO_00225.
DR   GeneID; 45134515; -.
DR   KEGG; cko:CKO_00225; -.
DR   HOGENOM; CLU_027494_0_1_6; -.
DR   OMA; YYDILTW; -.
DR   OrthoDB; 1444566at2; -.
DR   Proteomes; UP000008148; 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   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
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; IPR000189; Transglyc_AS.
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; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW   Reference proteome; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   CHAIN           33..515
FT                   /note="Membrane-bound lytic murein transglycosylase F"
FT                   /id="PRO_0000353923"
FT   REGION          33..269
FT                   /note="Non-LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   REGION          270..515
FT                   /note="LT domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
FT   REGION          493..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02016"
SQ   SEQUENCE   515 AA;  57911 MW;  1AE3D119A25F22A1 CRC64;
     MKKLKINYLF IGILTLLLAA ALWPSIPWFG KADNRIAAIQ SRGELRVSTI ESPLTYARIN
     GKKYGLDYEL AQQFASYLGV KLKITVRQNI SQLFDDLDNG NADLLAAGLV YNSERVKNYQ
     PGPTYYSVSQ QLVYRVGQYR PRTLATVNES QLSIAPGHVV VNDLQALKET KFPDLSWKVD
     DKKGTAALLS EVISGNLDYT IADSVAISLF QRVHPELAVA LDVTDEQPVT WFSQLDDDNT
     LSAALLDFFN TINEDGSLAR MEEKYLGHGD DFDYVDTRTF LRAVDGVLPD LQPLFEKYAQ
     EIDWRLLAAI SYQESHWDPL ATSPTGVRGL MMLTKNTAQS LGLTDRTDAE QSISGGVRYI
     QDMMGKVPET VPEEERIWFA LAAYNMGYAH MLDARALTVK TRGNPDSWAD VKQRLPLLSQ
     KQYYSKLTYG YARGHEAYAY VENIRKYQIS LVGYLQEKEK QAAEAIKLAQ DYPAVSPAEF
     DTETFPFSSF LSQPSSNYLS HSPSLPFSLK KKDEN