ID A0A143HKV1_9GAMM Unreviewed; 493 AA.
AC A0A143HKV1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Membrane-bound lytic murein transglycosylase F {ECO:0000256|HAMAP-Rule:MF_02016};
DE EC=4.2.2.n1 {ECO:0000256|HAMAP-Rule:MF_02016};
DE AltName: Full=Murein lyase F {ECO:0000256|HAMAP-Rule:MF_02016};
DE Flags: Precursor;
GN Name=mltF {ECO:0000256|HAMAP-Rule:MF_02016};
GN ORFNames=A3224_05450 {ECO:0000313|EMBL:AMX02100.1}, SAMN05660479_00294
GN {ECO:0000313|EMBL:SFB71448.1};
OS Microbulbifer thermotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX02100.1, ECO:0000313|Proteomes:UP000076077};
RN [1] {ECO:0000313|EMBL:AMX02100.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|EMBL:AMX02100.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA Lee Y.-S., Choi Y.-L.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFB71448.1, ECO:0000313|Proteomes:UP000181967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19189 {ECO:0000313|EMBL:SFB71448.1,
RC ECO:0000313|Proteomes:UP000181967};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_02016};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_02016}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02016}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral
CC membrane protein {ECO:0000256|ARBA:ARBA00004170}. Note=Attached to the
CC inner leaflet of the outer membrane. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02016}.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transglycosylase
CC Slt family. {ECO:0000256|HAMAP-Rule:MF_02016}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the bacterial solute-
CC binding protein 3 family. {ECO:0000256|HAMAP-Rule:MF_02016}.
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DR EMBL; CP014864; AMX02100.1; -; Genomic_DNA.
DR EMBL; FOKT01000001; SFB71448.1; -; Genomic_DNA.
DR RefSeq; WP_067152346.1; NZ_JAPHQH010000001.1.
DR AlphaFoldDB; A0A143HKV1; -.
DR STRING; 252514.A3224_05450; -.
DR GeneID; 76607496; -.
DR KEGG; mthd:A3224_05450; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000076077; Chromosome.
DR Proteomes; UP000181967; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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 CDD; cd13403; MLTF-like; 1.
DR CDD; cd01009; PBP2_YfhD_N; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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 PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR PANTHER; PTHR35936:SF32; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW Rule:MF_02016};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02016};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02016};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02016};
KW Reference proteome {ECO:0000313|Proteomes:UP000076077};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02016}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT CHAIN 22..493
FT /note="Membrane-bound lytic murein transglycosylase F"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT /id="PRO_5013972432"
FT DOMAIN 44..271
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT REGION 24..271
FT /note="Non-LT domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT REGION 272..493
FT /note="LT domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
FT ACT_SITE 318
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02016"
SQ SEQUENCE 493 AA; 55787 MW; C0DEE63B8E397375 CRC64;
MIMKSRIVRY SLRLAKGLVL AGCASLIVAS KTPDTLEQIK ASGKLIVLSQ NGPTTYYEDA
DGRHTGFEYG MLSAFAEELG VQLEIRDVHD LDEMFKRLRE PTEGAHLAAA GLTVTPERRE
QVRFTPSYFE IRQQVIYKIG EDRPRKVSDL EGKKVAVIAG SAHAEELRKL AQRHTDLEWE
EISDVDATEL LEMVNDGSYQ YAIVDSNAYA VHRGLYPNTA IAFNLTQFQP VAWAFPHSDD
DSLYRAARRF MLRANTSGLV AQLREEFFGH ISKLNAGGAQ AFAKSTRERL PQWREAMQKV
AEKYDLDWHL LAALSYQESH WNPRAKSPTG VRGLMMLTLD TARELGVNRL NPEQAIDGGA
RYFIKVRDKI PERIREPDRT WMALAAYNVG YGHLEDARIL TEKLGGNPDR WADVREHLPL
LAKRQYYKHT KHGYARGWEP VTYVQNIRHY QALLTWSSRI EEQRLAAAAE EAARELADNT
AVDMEAAAAA PAF
//
