ID   MLTA_VIBCH              Reviewed;         368 AA.
AC   Q9KPQ4;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Membrane-bound lytic murein transglycosylase A;
DE            EC=4.2.2.n1;
DE   AltName: Full=Murein hydrolase A;
DE   Flags: Precursor;
GN   Name=mltA; OrderedLocusNames=VC_2312;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division. Degrades
CC       murein glycan strands and insoluble, high-molecular weight murein
CC       sacculi (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR   EMBL; AE003852; AAF95456.1; -; Genomic_DNA.
DR   PIR; A82093; A82093.
DR   RefSeq; NP_231943.1; NC_002505.1.
DR   RefSeq; WP_000044381.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KPQ4; -.
DR   SMR; Q9KPQ4; -.
DR   STRING; 243277.VC_2312; -.
DR   CAZy; GH102; Glycoside Hydrolase Family 102.
DR   PRIDE; Q9KPQ4; -.
DR   DNASU; 2613108; -.
DR   EnsemblBacteria; AAF95456; AAF95456; VC_2312.
DR   GeneID; 57740931; -.
DR   KEGG; vch:VC_2312; -.
DR   PATRIC; fig|243277.26.peg.2204; -.
DR   eggNOG; COG2821; Bacteria.
DR   HOGENOM; CLU_037751_2_0_6; -.
DR   OMA; DQNGHPY; -.
DR   BioCyc; VCHO:VC2312-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IBA:GO_Central.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro.
DR   CDD; cd14485; mltA_like_LT_A; 1.
DR   Gene3D; 2.40.40.10; -; 1.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR026044; MltA.
DR   InterPro; IPR034654; MltA_3D.
DR   InterPro; IPR005300; MltA_B.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR30124; PTHR30124; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF03562; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Cell wall biogenesis/degradation; Lipoprotein; Lyase;
KW   Membrane; Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000305"
FT   CHAIN           17..368
FT                   /note="Membrane-bound lytic murein transglycosylase A"
FT                   /id="PRO_0000032783"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   368 AA;  40458 MW;  C1341A9D21A41DBB CRC64;
     MSKRLLSLAS LALLFGCAQQ PNDRAQQYQQ QTFPHILNRA DVVESNKPRD YTEFSKQSEL
     VVQGSASMAK IYRPLYEQLN EWVLQSGDPA TLAQFGIQAA QLGGGDKQGN VLFTGYFSPV
     IELRHQPDSV FKYPVYGLPK CNKNCPTRAE IYQGALDGQG LELGYAENLI DPFIMEVQGS
     GFVHFGDDDT LEYFAYAGKN NKAYVSIGKV LIERGLVERE KMSLKAIKDW VLANDEATVR
     ELLEENPSFV FFKPSAAAPV KGSAGIPLLP MASVAGDRSI LPMGTPILAE VPLLNADGTW
     SGAHQLRLLI VLDTGGAVKQ NHLDLYHGMG PRAGLEAGHY KHFGRVWKLG LENSPTQAPW
     ALPPEKQQ