ID F3G1V7_PSESJ Unreviewed; 438 AA.
AC F3G1V7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Membrane-bound lytic transglycosylase F {ECO:0000313|EMBL:EGH41057.1};
DE Flags: Fragment;
GN ORFNames=PSYPI_00915 {ECO:0000313|EMBL:EGH41057.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH41057.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH41057.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH41057.1,
RC ECO:0000313|Proteomes:UP000004986};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|ARBA:ARBA00004339}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004339}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGH41057.1}.
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DR EMBL; AEAI01000038; EGH41057.1; -; Genomic_DNA.
DR AlphaFoldDB; F3G1V7; -.
DR HOGENOM; CLU_027494_0_1_6; -.
DR Proteomes; UP000004986; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 50..275
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT NON_TER 438
FT /evidence="ECO:0000313|EMBL:EGH41057.1"
SQ SEQUENCE 438 AA; 49677 MW; 7B08961713053F3C CRC64;
MRFAYTAPMF FKPDFRPRCA KWLIATGLFL MLGACVEKPT TLERVKEDGV LRVITRNSPA
TYFQDRNGET GFEYELVKRF AKDLGVELKI ETADNLDDLF DQMNKPGGPV LGAAGLIETP
KRKSQARFSH SYLEVTPQVV YRNGQSRPTD PGDLVGKRIM VLKGSAHAEQ LAALKAQNPR
IEYEESDAVE VVDLLRMVDE GQLDLTLVDS NELAMNQVYF QNVRVAFDLG EARAQRWAVA
PGEDNSLLNE INAYLDKVEK NGTLQRLKDR YYGHVDVLGY VGAYTFAQHL QERLPKYEKH
FQTSAKKEQV DWRLLAAIGY QESMWQPTVT SKTGVRGLMM LTQNTAQAMG VSNRLDARQS
IQGGAKYFAY IKDQLDDSIK EPDRTWLALA SYNIGSGHLE DARKLAQNEG LNPDKWLDVK
KMLPRLAQKK WYSKTRYG
//
